The Biology of Lysosomes: From Order to Disorder
Since its discovery in 1955, the understanding of the lysosome has continuously increased. Once considered a mere waste removal system, the lysosome is now recognised as a highly crucial cellular component for signalling and energy metabolism. This notable evolution raises the need for a summarized...
Saved in:
| Published in: | Biomedicines Vol. 11; no. 1; p. 213 |
|---|---|
| Main Authors: | , , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
Switzerland
MDPI AG
14-01-2023
MDPI |
| Subjects: | |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Abstract | Since its discovery in 1955, the understanding of the lysosome has continuously increased. Once considered a mere waste removal system, the lysosome is now recognised as a highly crucial cellular component for signalling and energy metabolism. This notable evolution raises the need for a summarized review of the lysosome's biology. As such, throughout this article, we will be compiling the current knowledge regarding the lysosome's biogenesis and functions. The comprehension of this organelle's inner mechanisms is crucial to perceive how its impairment can give rise to lysosomal disease (LD). In this review, we highlight some examples of LD fine-tuned mechanisms that are already established, as well as others, which are still under investigation. Even though the understanding of the lysosome and its pathologies has expanded through the years, some of its intrinsic molecular aspects remain unknown. In order to illustrate the complexity of the lysosomal diseases we provide a few examples that have challenged the established single gene-single genetic disorder model. As such, we believe there is a strong need for further investigation of the exact abnormalities in the pathological pathways in lysosomal disease. |
|---|---|
| AbstractList | Since its discovery in 1955, the understanding of the lysosome has continuously increased. Once considered a mere waste removal system, the lysosome is now recognised as a highly crucial cellular component for signalling and energy metabolism. This notable evolution raises the need for a summarized review of the lysosome’s biology. As such, throughout this article, we will be compiling the current knowledge regarding the lysosome’s biogenesis and functions. The comprehension of this organelle’s inner mechanisms is crucial to perceive how its impairment can give rise to lysosomal disease (LD). In this review, we highlight some examples of LD fine-tuned mechanisms that are already established, as well as others, which are still under investigation. Even though the understanding of the lysosome and its pathologies has expanded through the years, some of its intrinsic molecular aspects remain unknown. In order to illustrate the complexity of the lysosomal diseases we provide a few examples that have challenged the established single gene—single genetic disorder model. As such, we believe there is a strong need for further investigation of the exact abnormalities in the pathological pathways in lysosomal disease. Since its discovery in 1955, the understanding of the lysosome has continuously increased. Once considered a mere waste removal system, the lysosome is now recognised as a highly crucial cellular component for signalling and energy metabolism. This notable evolution raises the need for a summarized review of the lysosome's biology. As such, throughout this article, we will be compiling the current knowledge regarding the lysosome's biogenesis and functions. The comprehension of this organelle's inner mechanisms is crucial to perceive how its impairment can give rise to lysosomal disease (LD). In this review, we highlight some examples of LD fine-tuned mechanisms that are already established, as well as others, which are still under investigation. Even though the understanding of the lysosome and its pathologies has expanded through the years, some of its intrinsic molecular aspects remain unknown. In order to illustrate the complexity of the lysosomal diseases we provide a few examples that have challenged the established single gene-single genetic disorder model. As such, we believe there is a strong need for further investigation of the exact abnormalities in the pathological pathways in lysosomal disease.Since its discovery in 1955, the understanding of the lysosome has continuously increased. Once considered a mere waste removal system, the lysosome is now recognised as a highly crucial cellular component for signalling and energy metabolism. This notable evolution raises the need for a summarized review of the lysosome's biology. As such, throughout this article, we will be compiling the current knowledge regarding the lysosome's biogenesis and functions. The comprehension of this organelle's inner mechanisms is crucial to perceive how its impairment can give rise to lysosomal disease (LD). In this review, we highlight some examples of LD fine-tuned mechanisms that are already established, as well as others, which are still under investigation. Even though the understanding of the lysosome and its pathologies has expanded through the years, some of its intrinsic molecular aspects remain unknown. In order to illustrate the complexity of the lysosomal diseases we provide a few examples that have challenged the established single gene-single genetic disorder model. As such, we believe there is a strong need for further investigation of the exact abnormalities in the pathological pathways in lysosomal disease. |
| Author | Amaral, Olga Mondragão-Rodrigues, Inês Martins, Mariana Duarte, Ana Joana Oliveira, Ana Rita Macedo, M Fátima |
| AuthorAffiliation | 2 Centro de Estudos de Ciência Animal (CECA, ICETA), Universidade do Porto, 4485-661 Porto, Portugal 5 Instituto de Ciências Biomédicas Abel Salazar (ICBAS), Universidade do Porto, 4050-313 Porto, Portugal 6 CAGE, Instituto de Investigação e Inovação em Saúde (i3S), Universidade do Porto, Rua Alfredo Allen, 208, 4200-135 Porto, Portugal 3 Laboratório Associado para Ciência Animal e Veterinária (AL4AnimalS), 1300-477 Lisboa, Portugal 4 Departamento de Ciências Médicas, Universidade de Aveiro, Campus Universitário de Santiago, Agra do Crasto, Edifício 30, 3810-193 Aveiro, Portugal 1 Departamento de Genética Humana, Unidade de Investigação e Desenvolvimento, Instituto Nacional de Saúde Ricardo Jorge (INSA), 4000-055 Porto, Portugal |
| AuthorAffiliation_xml | – name: 6 CAGE, Instituto de Investigação e Inovação em Saúde (i3S), Universidade do Porto, Rua Alfredo Allen, 208, 4200-135 Porto, Portugal – name: 1 Departamento de Genética Humana, Unidade de Investigação e Desenvolvimento, Instituto Nacional de Saúde Ricardo Jorge (INSA), 4000-055 Porto, Portugal – name: 4 Departamento de Ciências Médicas, Universidade de Aveiro, Campus Universitário de Santiago, Agra do Crasto, Edifício 30, 3810-193 Aveiro, Portugal – name: 5 Instituto de Ciências Biomédicas Abel Salazar (ICBAS), Universidade do Porto, 4050-313 Porto, Portugal – name: 3 Laboratório Associado para Ciência Animal e Veterinária (AL4AnimalS), 1300-477 Lisboa, Portugal – name: 2 Centro de Estudos de Ciência Animal (CECA, ICETA), Universidade do Porto, 4485-661 Porto, Portugal |
| Author_xml | – sequence: 1 givenname: Olga surname: Amaral fullname: Amaral, Olga organization: Laboratório Associado para Ciência Animal e Veterinária (AL4AnimalS), 1300-477 Lisboa, Portugal – sequence: 2 givenname: Mariana surname: Martins fullname: Martins, Mariana organization: Departamento de Ciências Médicas, Universidade de Aveiro, Campus Universitário de Santiago, Agra do Crasto, Edifício 30, 3810-193 Aveiro, Portugal – sequence: 3 givenname: Ana Rita surname: Oliveira fullname: Oliveira, Ana Rita organization: Departamento de Ciências Médicas, Universidade de Aveiro, Campus Universitário de Santiago, Agra do Crasto, Edifício 30, 3810-193 Aveiro, Portugal – sequence: 4 givenname: Ana Joana surname: Duarte fullname: Duarte, Ana Joana organization: Instituto de Ciências Biomédicas Abel Salazar (ICBAS), Universidade do Porto, 4050-313 Porto, Portugal – sequence: 5 givenname: Inês orcidid: 0000-0002-1425-1498 surname: Mondragão-Rodrigues fullname: Mondragão-Rodrigues, Inês organization: CAGE, Instituto de Investigação e Inovação em Saúde (i3S), Universidade do Porto, Rua Alfredo Allen, 208, 4200-135 Porto, Portugal – sequence: 6 givenname: M Fátima orcidid: 0000-0002-2252-6105 surname: Macedo fullname: Macedo, M Fátima organization: CAGE, Instituto de Investigação e Inovação em Saúde (i3S), Universidade do Porto, Rua Alfredo Allen, 208, 4200-135 Porto, Portugal |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/36672721$$D View this record in MEDLINE/PubMed |
| BookMark | eNptkctOHDEQRa2IKMCEP4hQS2yyGeJH-ZUFEuGRII3Ehqwtd3d58KinDXZPpPn7dDOAIIo3LpVvHV3fOiR7feqRkC-Mngph6bc6pjW2sYk9FsYoo5yJD-SAc67nlkq796beJ0elrOh4LBOGwSeyL5TSXHN2QOjdPVY_YurSclulUC22JZWRXb5X1zmtq9vcYq6GVF3Gkqb6M_kYfFfw6Pmekd_XV3cXv-aL2583F-eLeSMFHebAUVL0StY6aAs1sBCoDuiDbKFRzHrNghcwmrBcSm8ZUGyRWWgg0FqIGbnZcdvkV-4hx7XPW5d8dE-NlJfO5yE2HTqgrZCKm8ChBcpqw5U3NXgDQA2EMLLOdqyHTT3G1mA_ZN-9g75_6eO9W6Y_zhqppmhn5OszIKfHDZbBrWNpsOt8j2lTHNfKcG6UnXyf_CNdpU3ux6gmlWaGg6WjCnaqJqdSMoZXM4y6acPufxsex47ffuR16GWf4i-1qKRL |
| CitedBy_id | crossref_primary_10_3389_fcell_2024_1386149 crossref_primary_10_3390_biomedicines12010174 crossref_primary_10_3390_ijms242115613 crossref_primary_10_1016_j_aqrep_2023_101645 crossref_primary_10_1016_j_ijbiomac_2024_130451 |
| Cites_doi | 10.3390/cells11193153 10.1038/ncb1753 10.1111/j.1582-4934.2009.00973.x 10.1126/science.aag1417 10.1111/ncn3.12554 10.1146/annurev.genom.9.081307.164303 10.1093/hmg/ddt052 10.1101/cshperspect.a016790 10.1093/hmg/ddr306 10.1016/j.devcel.2013.08.003 10.1515/bchm3.1988.369.1.317 10.1073/pnas.1424288112 10.1016/bs.mie.2017.06.004 10.1016/S0014-5793(02)03670-0 10.1111/tra.12056 10.1038/ncb3114 10.1016/j.cell.2007.10.018 10.1016/S0002-9297(07)62941-3 10.1186/s13041-019-0439-2 10.1016/0092-8674(91)90459-C 10.1590/1678-4685-gmb-2018-0159 10.1083/jcb.149.5.1053 10.1111/j.1399-0004.2007.00899.x 10.1038/s41467-017-01871-z 10.1016/j.aninu.2021.05.003 10.3390/cells8070727 10.1146/annurev-med-122313-085916 10.1007/8904_2015_469 10.1073/pnas.61.2.484 10.1038/emboj.2010.237 10.1083/jcb.141.2.359 10.1186/s12964-021-00730-1 10.1007/978-3-319-96704-2_6 10.1016/j.nbd.2018.05.015 10.1126/scisignal.2004754 10.1091/mbc.e08-12-1248 10.1016/j.ymgme.2004.04.011 10.1083/jcb.104.6.1735 10.1016/0014-5793(91)81211-P 10.1093/hmg/ddq204 10.1007/978-1-4939-9018-4_12 10.4161/auto.5227 10.1111/j.1600-0854.2005.00337.x 10.3390/ijms21103448 10.1007/s00418-008-0384-0 10.1146/annurev-physiol-012110-142317 10.1016/j.bbamcr.2008.10.016 10.1016/bs.irn.2020.02.012 10.1038/ncb0905-847 10.1126/sciimmunol.aak9573 10.1038/nature21368 10.1091/mbc.e02-02-0114 10.1016/j.bbamcr.2008.12.001 10.1091/mbc.e05-03-0213 10.1038/s41573-019-0036-1 10.1002/humu.21566 10.1111/j.1365-2141.2004.05351.x 10.1177/2326409813517663 10.1126/science.abg6621 10.1146/annurev.cellbio.21.122303.120013 10.1007/s13311-019-00742-3 10.1016/j.ebiom.2020.103166 10.1038/79095 10.3390/cells10020333 10.1038/s41572-018-0025-4 10.1146/annurev-physiol-021014-071649 10.1007/s00401-015-1385-4 10.1083/jcb.137.5.1161 10.1053/ejpn.2000.0428 10.1016/S0092-8674(03)00347-7 10.1083/jcb.200308038 10.1186/s12964-020-00619-5 10.1016/j.bbamcr.2008.11.015 10.1038/ncomms12109 10.1007/978-3-642-74415-0 10.1083/jcb.201208152 10.1186/s13578-020-00489-x 10.1038/nrneurol.2013.163 10.1038/nature24035 10.1371/journal.pone.0182895 10.1016/j.bbrc.2003.12.092 10.1038/nrd.2017.214 10.1038/35022604 10.3390/biom7030051 10.1016/j.febslet.2009.12.056 10.1126/science.1174447 10.1074/jbc.270.45.27311 10.1016/0006-291X(65)90743-6 10.1038/25133 10.1126/stke.2722005re3 10.1126/science.2842863 10.1016/0092-8674(95)90314-3 10.1038/nrm3565 10.1126/science.1204592 10.1016/bs.ircmb.2021.03.002 10.1006/bbrc.1995.2528 10.1073/pnas.95.11.6373 10.1242/jcs.184770 10.1038/nrm1985 10.1016/j.kint.2015.12.045 10.1038/nature09076 10.3389/fcell.2020.609683 10.1111/j.1600-0854.2008.00701.x 10.1111/jnc.14462 10.1101/cshperspect.a016840 10.1146/annurev-cellbio-101512-122326 10.1042/BJ20110949 10.1212/WNL.31.1.51 10.1038/nrm2217 10.1038/ncomms1037 10.1016/j.bcp.2022.115229 10.1074/jbc.R110.134452 10.1038/cdd.2008.168 10.1016/j.ijep.2017.08.001 10.1186/s40478-016-0324-5 10.1002/1097-0134(20001115)41:3<374::AID-PROT90>3.0.CO;2-F 10.1038/jhg.2012.72 10.1111/j.1600-0854.2006.00475.x 10.1093/hmg/ddn124 10.1146/annurev.biochem.72.121801.161800 10.1016/j.cell.2017.03.035 10.1242/jcs.221739 10.1007/s10753-021-01415-0 10.1016/j.cub.2005.01.049 10.1016/j.mam.2006.08.005 10.1016/j.bbrc.2016.09.093 10.1016/S0962-8924(03)00005-9 10.1038/nrm2745 10.1016/j.devcel.2011.07.016 10.1016/j.neuron.2014.09.034 |
| ContentType | Journal Article |
| Copyright | 2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 2023 by the authors. 2023 |
| Copyright_xml | – notice: 2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. – notice: 2023 by the authors. 2023 |
| DBID | NPM AAYXX CITATION 8FE 8FH ABUWG AFKRA AZQEC BBNVY BENPR BHPHI CCPQU DWQXO GNUQQ HCIFZ LK8 M7P PIMPY PQEST PQQKQ PQUKI PRINS 7X8 5PM DOA |
| DOI | 10.3390/biomedicines11010213 |
| DatabaseName | PubMed CrossRef ProQuest SciTech Collection ProQuest Natural Science Collection ProQuest Central (Alumni) ProQuest Central UK/Ireland ProQuest Central Essentials Biological Science Collection ProQuest Central ProQuest Natural Science Collection ProQuest One Community College ProQuest Central ProQuest Central Student SciTech Premium Collection ProQuest Biological Science Collection Biological Science Database Publicly Available Content (ProQuest) ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China MEDLINE - Academic PubMed Central (Full Participant titles) Directory of Open Access Journals |
| DatabaseTitle | PubMed CrossRef Publicly Available Content Database ProQuest Central Student ProQuest Biological Science Collection ProQuest Central Essentials ProQuest One Academic Eastern Edition ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest Natural Science Collection Biological Science Database ProQuest SciTech Collection ProQuest Central China ProQuest Central ProQuest One Academic UKI Edition Natural Science Collection ProQuest Central Korea Biological Science Collection ProQuest One Academic MEDLINE - Academic |
| DatabaseTitleList | Publicly Available Content Database MEDLINE - Academic PubMed CrossRef |
| Database_xml | – sequence: 1 dbid: DOA name: Directory of Open Access Journals url: http://www.doaj.org/ sourceTypes: Open Website |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Engineering Biology |
| EISSN | 2227-9059 |
| ExternalDocumentID | oai_doaj_org_article_40d35628f24d401b826a8b4a844084ff 10_3390_biomedicines11010213 36672721 |
| Genre | Journal Article Review |
| GroupedDBID | 53G 5VS 8FE 8FH AADQD AAFWJ ACPRK ADBBV AFKRA AFPKN AFZYC ALMA_UNASSIGNED_HOLDINGS AOIJS BBNVY BCNDV BENPR BHPHI CCPQU EMOBN GROUPED_DOAJ GX1 HCIFZ HYE IAO IHR INH ITC KQ8 LK8 M7P MODMG M~E NPM OK1 PGMZT PIMPY PROAC RPM AAYXX CITATION ABUWG AZQEC DWQXO GNUQQ PQEST PQQKQ PQUKI PRINS 7X8 5PM |
| ID | FETCH-LOGICAL-c530t-42e50ea65b7f794b41ff07feaf5d4c619a71fa347219255a9140ede194c4f0b33 |
| IEDL.DBID | RPM |
| ISSN | 2227-9059 |
| IngestDate | Tue Oct 22 15:14:56 EDT 2024 Tue Sep 17 21:30:40 EDT 2024 Sat Oct 26 03:59:55 EDT 2024 Thu Oct 10 17:49:04 EDT 2024 Fri Nov 22 02:25:19 EST 2024 Sat Nov 02 12:12:06 EDT 2024 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 1 |
| Keywords | lysosome biogenesis and function endocytic pathway lysosome lysosomal disease |
| Language | English |
| License | Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c530t-42e50ea65b7f794b41ff07feaf5d4c619a71fa347219255a9140ede194c4f0b33 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 These authors contributed equally to this work. |
| ORCID | 0000-0002-2252-6105 0000-0002-1425-1498 |
| OpenAccessLink | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9856021/ |
| PMID | 36672721 |
| PQID | 2767182490 |
| PQPubID | 2032426 |
| ParticipantIDs | doaj_primary_oai_doaj_org_article_40d35628f24d401b826a8b4a844084ff pubmedcentral_primary_oai_pubmedcentral_nih_gov_9856021 proquest_miscellaneous_2768228693 proquest_journals_2767182490 crossref_primary_10_3390_biomedicines11010213 pubmed_primary_36672721 |
| PublicationCentury | 2000 |
| PublicationDate | 2023-01-14 |
| PublicationDateYYYYMMDD | 2023-01-14 |
| PublicationDate_xml | – month: 01 year: 2023 text: 2023-01-14 day: 14 |
| PublicationDecade | 2020 |
| PublicationPlace | Switzerland |
| PublicationPlace_xml | – name: Switzerland – name: Basel |
| PublicationTitle | Biomedicines |
| PublicationTitleAlternate | Biomedicines |
| PublicationYear | 2023 |
| Publisher | MDPI AG MDPI |
| Publisher_xml | – name: MDPI AG – name: MDPI |
| References | Tang (ref_83) 2020; 10 Schnabel (ref_128) 1991; 290 Saxton (ref_48) 2017; 169 Machleidt (ref_98) 1988; 369 ref_90 Terasawa (ref_114) 2016; 479 ref_13 ref_130 Settembre (ref_10) 2013; 14 ref_95 (ref_1) 2005; 7 Vaccaro (ref_104) 2010; 19 Bonam (ref_80) 2019; 18 Alaei (ref_100) 2019; 13 Fraldi (ref_96) 2010; 29 Parenti (ref_91) 2015; 66 Traub (ref_39) 2013; 5 Bargal (ref_64) 2000; 26 Pryor (ref_139) 2006; 7 Wong (ref_110) 2004; 82 Nishino (ref_119) 2000; 406 Saftig (ref_15) 2009; 10 ref_126 ref_125 Vairo (ref_4) 2019; 42 Boudewyn (ref_65) 2019; 148 Janvier (ref_38) 2005; 16 Eskelinen (ref_115) 2002; 13 Raffaello (ref_69) 2019; Volume 1925 Peng (ref_85) 2019; 16 Pandey (ref_107) 2017; 543 Bright (ref_34) 2005; 15 Rowland (ref_137) 2016; 129 Winchester (ref_41) 2001; 5 Danon (ref_89) 1981; 31 ref_29 Koh (ref_87) 2019; 12 Madhyastha (ref_30) 2021; 44 Peters (ref_122) 1998; 396 Xu (ref_2) 2015; 77 ref_71 Eskelinen (ref_112) 2006; 27 Platt (ref_3) 2018; 4 Cheng (ref_123) 2010; 584 Alroy (ref_5) 2014; 2 Platt (ref_92) 2018; 17 ref_78 Medina (ref_68) 2015; 17 Colombo (ref_25) 2014; 30 Jahreiss (ref_35) 2008; 9 Eskelinen (ref_118) 2005; 6 Lee (ref_106) 1968; 61 Stoorvogel (ref_22) 1991; 65 LaPlante (ref_45) 2002; 532 Marques (ref_47) 2019; 132 Braulke (ref_14) 2009; 1793 Balreira (ref_103) 2008; 17 Komura (ref_127) 2017; Volume 597 Zhang (ref_54) 2021; 7 Czartoryska (ref_105) 2007; 72 ref_86 Vitner (ref_8) 2010; 285 Luzio (ref_31) 2014; 6 Hirota (ref_33) 2004; 314 Kolter (ref_9) 2005; 21 Gurung (ref_26) 2021; 19 Castellano (ref_51) 2017; 355 Peng (ref_28) 2020; 18 Bretou (ref_67) 2017; 2 Sullivan (ref_88) 2016; 4 Dierks (ref_133) 2003; 113 Bonifacino (ref_37) 2003; 72 Lamaze (ref_56) 2018; Volume 57 Velayati (ref_102) 2011; 32 Braulke (ref_20) 1987; 104 Almeida (ref_84) 2020; Volume 154 Endo (ref_120) 2015; 129 Chen (ref_63) 2017; 550 Medina (ref_60) 2021; Volume 362 ref_53 Yu (ref_36) 2010; 465 Ballabio (ref_7) 2009; 1793 Kretz (ref_99) 1988; 241 Cheng (ref_111) 2012; 57 Dierks (ref_131) 2009; 1793 Willett (ref_77) 2017; 8 Meel (ref_19) 2008; 129 Lipton (ref_81) 2014; 84 Rosado (ref_55) 2016; Volume 898 Morgan (ref_57) 2011; 439 Schmidt (ref_132) 1995; 82 Settembre (ref_12) 2011; 332 Platt (ref_93) 2012; 199 Morava (ref_129) 2015; Volume 25 Eskelinen (ref_42) 2003; 13 Lie (ref_82) 2019; 122 Chen (ref_140) 1998; 95 Luzio (ref_23) 2007; 8 Contreras (ref_73) 2021; 8 Ghosh (ref_18) 2003; 163 Pryor (ref_32) 2000; 149 Bassi (ref_44) 2000; 67 Zhang (ref_61) 2016; 7 Huizing (ref_46) 2008; 9 Guo (ref_117) 2019; 18 Bonifacino (ref_24) 2006; 7 Chen (ref_79) 2015; 7 Wang (ref_59) 2015; 112 Boustany (ref_6) 2013; 9 Kim (ref_50) 2008; 10 Konecki (ref_121) 1995; 215 Yang (ref_101) 2015; 112 Sardiello (ref_75) 2009; 325 Yadin (ref_138) 2022; 204 Schneede (ref_116) 2011; 15 Schwake (ref_40) 2013; 14 Pohlmann (ref_21) 1995; 270 Klumperman (ref_16) 1998; 141 Kochumon (ref_124) 2017; 04 Sugie (ref_136) 2022; 10 Rega (ref_72) 2016; 89 Medina (ref_70) 2011; 21 Mindell (ref_58) 2012; 74 Sidransky (ref_108) 2012; 14 Jmoudiak (ref_135) 2005; 129 Palmieri (ref_11) 2011; 20 Bowman (ref_17) 2000; 41 Fader (ref_27) 2009; 16 Song (ref_74) 2021; 25 Settembre (ref_97) 2008; 4 ref_109 Dong (ref_62) 2010; 1 Shin (ref_52) 2022; 377 Hosokawa (ref_49) 2009; 20 Gough (ref_113) 1997; 137 Reczek (ref_43) 2007; 131 Song (ref_76) 2013; 22 Brady (ref_134) 1965; 18 Samie (ref_66) 2013; 26 Myerowitz (ref_94) 2021; 63 |
| References_xml | – ident: ref_71 doi: 10.3390/cells11193153 – volume: 10 start-page: 935 year: 2008 ident: ref_50 article-title: Regulation of TORC1 by Rag GTPases in nutrient response publication-title: Nat. Cell Biol. doi: 10.1038/ncb1753 contributor: fullname: Kim – volume: 15 start-page: 280 year: 2011 ident: ref_116 article-title: Role for LAMP-2 in endosomal cholesterol transport publication-title: J. Cell. Mol. Med. doi: 10.1111/j.1582-4934.2009.00973.x contributor: fullname: Schneede – volume: 355 start-page: 1306 year: 2017 ident: ref_51 article-title: Lysosomal cholesterol activates mTORC1 via an SLC38A9–Niemann-Pick C1 signaling complex publication-title: Science doi: 10.1126/science.aag1417 contributor: fullname: Castellano – volume: 10 start-page: 273 year: 2022 ident: ref_136 article-title: Autophagic vacuolar myopathy: Danon disease and related myopathies publication-title: Neurol. Clin. Neurosci. doi: 10.1111/ncn3.12554 contributor: fullname: Sugie – volume: 9 start-page: 359 year: 2008 ident: ref_46 article-title: Disorders of Lysosome-Related Organelle Biogenesis: Clinical and Molecular Genetics publication-title: Annu. Rev. Genomics Hum. Genet. doi: 10.1146/annurev.genom.9.081307.164303 contributor: fullname: Huizing – volume: 22 start-page: 1994 year: 2013 ident: ref_76 article-title: TFEB regulates lysosomal proteostasis publication-title: Hum. Mol. Genet. doi: 10.1093/hmg/ddt052 contributor: fullname: Song – volume: 5 start-page: a016790 year: 2013 ident: ref_39 article-title: Cargo Recognition in Clathrin-Mediated Endocytosis publication-title: Cold Spring Harb. Perspect. Biol. doi: 10.1101/cshperspect.a016790 contributor: fullname: Traub – volume: 20 start-page: 3852 year: 2011 ident: ref_11 article-title: Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways publication-title: Hum. Mol. Genet. doi: 10.1093/hmg/ddr306 contributor: fullname: Palmieri – volume: 112 start-page: E1373 year: 2015 ident: ref_59 article-title: Up-regulation of lysosomal TRPML1 channels is essential for lysosomal adaptation to nutrient starvation publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Wang – volume: 26 start-page: 511 year: 2013 ident: ref_66 article-title: A TRP Channel in the Lysosome Regulates Large Particle Phagocytosis via Focal Exocytosis publication-title: Dev. Cell doi: 10.1016/j.devcel.2013.08.003 contributor: fullname: Samie – volume: 369 start-page: 317 year: 1988 ident: ref_98 article-title: The Precursor of Sulfatide Activator Protein is Processed to Three Different Proteins publication-title: Biol. Chem. Hoppe. Seyler doi: 10.1515/bchm3.1988.369.1.317 contributor: fullname: Machleidt – volume: 112 start-page: 1137 year: 2015 ident: ref_101 article-title: Mutant glucocerebrosidase in Gaucher disease recruits Hsp27 to the Hsp90 chaperone complex for proteasomal degradation publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1424288112 contributor: fullname: Yang – volume: Volume 597 start-page: 239 year: 2017 ident: ref_127 article-title: Syntheses of Fluorescent Gangliosides for the Studies of Raft Domains publication-title: Methods in Enzymology doi: 10.1016/bs.mie.2017.06.004 contributor: fullname: Komura – volume: 532 start-page: 183 year: 2002 ident: ref_45 article-title: Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway publication-title: FEBS Lett. doi: 10.1016/S0014-5793(02)03670-0 contributor: fullname: LaPlante – volume: 14 start-page: 739 year: 2013 ident: ref_40 article-title: Lysosomal Membrane Proteins and Their Central Role in Physiology: Lysosomal Membrane Proteins publication-title: Traffic doi: 10.1111/tra.12056 contributor: fullname: Schwake – volume: 17 start-page: 288 year: 2015 ident: ref_68 article-title: Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB publication-title: Nat. Cell Biol. doi: 10.1038/ncb3114 contributor: fullname: Medina – volume: 131 start-page: 770 year: 2007 ident: ref_43 article-title: LIMP-2 Is a Receptor for Lysosomal Mannose-6-Phosphate-Independent Targeting of β-Glucocerebrosidase publication-title: Cell doi: 10.1016/j.cell.2007.10.018 contributor: fullname: Reczek – volume: 67 start-page: 1110 year: 2000 ident: ref_44 article-title: Cloning of the Gene Encoding a Novel Integral Membrane Protein, Mucolipidin—and Identification of the Two Major Founder Mutations Causing Mucolipidosis Type IV publication-title: Am. J. Hum. Genet. doi: 10.1016/S0002-9297(07)62941-3 contributor: fullname: Bassi – volume: 12 start-page: 18 year: 2019 ident: ref_87 article-title: Lysosomal dysfunction in proteinopathic neurodegenerative disorders: Possible therapeutic roles of cAMP and zinc publication-title: Mol. Brain doi: 10.1186/s13041-019-0439-2 contributor: fullname: Koh – volume: 65 start-page: 417 year: 1991 ident: ref_22 article-title: Late endosomes derive from early endosomes by maturation publication-title: Cell doi: 10.1016/0092-8674(91)90459-C contributor: fullname: Stoorvogel – volume: 42 start-page: 165 year: 2019 ident: ref_4 article-title: Lysosomal diseases: Overview on current diagnosis and treatment publication-title: Genet. Mol. Biol. doi: 10.1590/1678-4685-gmb-2018-0159 contributor: fullname: Vairo – volume: 149 start-page: 10 year: 2000 ident: ref_32 article-title: The Role of Intraorganellar Ca2+ in Late Endosome–Lysosome Heterotypic Fusion and in the Reformation of Lysosomes from Hybrid Organelles publication-title: J. Cell Biol. doi: 10.1083/jcb.149.5.1053 contributor: fullname: Pryor – volume: 72 start-page: 538 year: 2007 ident: ref_105 article-title: Non-neuronopathic Gaucher disease due to saposin C deficiency publication-title: Clin. Genet. doi: 10.1111/j.1399-0004.2007.00899.x contributor: fullname: Czartoryska – volume: 8 start-page: 1580 year: 2017 ident: ref_77 article-title: TFEB regulates lysosomal positioning by modulating TMEM55B expression and JIP4 recruitment to lysosomes publication-title: Nat. Commun. doi: 10.1038/s41467-017-01871-z contributor: fullname: Willett – volume: 7 start-page: 1009 year: 2021 ident: ref_54 article-title: Regulation of mTORC1 by amino acids in mammalian cells: A general picture of recent advances publication-title: Anim. Nutr. doi: 10.1016/j.aninu.2021.05.003 contributor: fullname: Zhang – ident: ref_29 doi: 10.3390/cells8070727 – volume: 66 start-page: 471 year: 2015 ident: ref_91 article-title: Lysosomal Storage Diseases: From Pathophysiology to Therapy publication-title: Annu. Rev. Med. doi: 10.1146/annurev-med-122313-085916 contributor: fullname: Parenti – volume: Volume 25 start-page: 83 year: 2015 ident: ref_129 article-title: GM2-Gangliosidosis, AB Variant: Clinical, Ophthalmological, MRI, and Molecular Findings publication-title: JIMD Reports, Volume 25 doi: 10.1007/8904_2015_469 contributor: fullname: Morava – volume: 61 start-page: 484 year: 1968 ident: ref_106 article-title: The fine structure of the cerebroside occurring in Gaucher’s disease publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.61.2.484 contributor: fullname: Lee – volume: 29 start-page: 3607 year: 2010 ident: ref_96 article-title: Lysosomal fusion and SNARE function are impaired by cholesterol accumulation in lysosomal storage disorders publication-title: EMBO J. doi: 10.1038/emboj.2010.237 contributor: fullname: Fraldi – volume: 141 start-page: 359 year: 1998 ident: ref_16 article-title: Mannose 6–Phosphate Receptors Are Sorted from Immature Secretory Granules via Adaptor Protein AP-1, Clathrin, and Syntaxin 6–positive Vesicles publication-title: J. Cell Biol. doi: 10.1083/jcb.141.2.359 contributor: fullname: Klumperman – volume: 19 start-page: 47 year: 2021 ident: ref_26 article-title: The exosome journey: From biogenesis to uptake and intracellular signalling publication-title: Cell Commun. Signal. doi: 10.1186/s12964-021-00730-1 contributor: fullname: Gurung – volume: Volume 57 start-page: 151 year: 2018 ident: ref_56 article-title: The Lysosome and Intracellular Signalling publication-title: Endocytosis and Signaling doi: 10.1007/978-3-319-96704-2_6 contributor: fullname: Lamaze – volume: 122 start-page: 94 year: 2019 ident: ref_82 article-title: Lysosome trafficking and signaling in health and neurodegenerative diseases publication-title: Neurobiol. Dis. doi: 10.1016/j.nbd.2018.05.015 contributor: fullname: Lie – ident: ref_13 doi: 10.1126/scisignal.2004754 – volume: 20 start-page: 1981 year: 2009 ident: ref_49 article-title: Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy publication-title: Mol. Biol. Cell doi: 10.1091/mbc.e08-12-1248 contributor: fullname: Hosokawa – volume: 82 start-page: 192 year: 2004 ident: ref_110 article-title: Neuropathology provides clues to the pathophysiology of Gaucher disease publication-title: Mol. Genet. Metab. doi: 10.1016/j.ymgme.2004.04.011 contributor: fullname: Wong – volume: 104 start-page: 1735 year: 1987 ident: ref_20 article-title: Is movement of mannose 6-phosphate-specific receptor triggered by binding of lysosomal enzymes? publication-title: J. Cell Biol. doi: 10.1083/jcb.104.6.1735 contributor: fullname: Braulke – volume: 290 start-page: 1 year: 1991 ident: ref_128 article-title: A mutation in the gene of a glycolipid-binding protein (GM2 activator) that causes GM2-gangliosidosis variant AB publication-title: FEBS Lett. doi: 10.1016/0014-5793(91)81211-P contributor: fullname: Schnabel – volume: 19 start-page: 2987 year: 2010 ident: ref_104 article-title: Saposin C mutations in Gaucher disease patients resulting in lysosomal lipid accumulation, saposin C deficiency, but normal prosaposin processing and sorting publication-title: Hum. Mol. Genet. doi: 10.1093/hmg/ddq204 contributor: fullname: Vaccaro – volume: Volume 1925 start-page: 143 year: 2019 ident: ref_69 article-title: TRPML1-/TFEB-Dependent Regulation of Lysosomal Exocytosis publication-title: Calcium Signalling doi: 10.1007/978-1-4939-9018-4_12 contributor: fullname: Raffaello – volume: Volume 898 start-page: 423 year: 2016 ident: ref_55 article-title: Modulation of Calcium Entry by the Endo-lysosomal System publication-title: Calcium Entry Pathways in Non-Excitable Cells contributor: fullname: Rosado – volume: 4 start-page: 113 year: 2008 ident: ref_97 article-title: Lysosomal storage diseases as disorders of autophagy publication-title: Autophagy doi: 10.4161/auto.5227 contributor: fullname: Settembre – volume: 6 start-page: 1058 year: 2005 ident: ref_118 article-title: Unifying Nomenclature for the Isoforms of the Lysosomal Membrane Protein LAMP-2: LAMP-2 Isoform Nomenclature publication-title: Traffic doi: 10.1111/j.1600-0854.2005.00337.x contributor: fullname: Eskelinen – ident: ref_95 doi: 10.3390/ijms21103448 – volume: 129 start-page: 253 year: 2008 ident: ref_19 article-title: Imaging and imagination: Understanding the endo-lysosomal system publication-title: Histochem. Cell Biol. doi: 10.1007/s00418-008-0384-0 contributor: fullname: Meel – volume: 74 start-page: 69 year: 2012 ident: ref_58 article-title: Lysosomal Acidification Mechanisms publication-title: Annu. Rev. Physiol. doi: 10.1146/annurev-physiol-012110-142317 contributor: fullname: Mindell – volume: 1793 start-page: 605 year: 2009 ident: ref_14 article-title: Sorting of lysosomal proteins publication-title: Biochim. Biophys. Acta BBA Mol. Cell Res. doi: 10.1016/j.bbamcr.2008.10.016 contributor: fullname: Braulke – volume: Volume 154 start-page: 303 year: 2020 ident: ref_84 article-title: Endosomal-lysosomal dysfunction in metabolic diseases and Alzheimer’s disease publication-title: International Review of Neurobiology doi: 10.1016/bs.irn.2020.02.012 contributor: fullname: Almeida – volume: 7 start-page: 847 year: 2005 ident: ref_1 article-title: The lysosome turns fifty publication-title: Nat. Cell Biol. doi: 10.1038/ncb0905-847 – volume: 2 start-page: eaak9573 year: 2017 ident: ref_67 article-title: Lysosome signaling controls the migration of dendritic cells publication-title: Sci. Immunol. doi: 10.1126/sciimmunol.aak9573 contributor: fullname: Bretou – volume: 543 start-page: 108 year: 2017 ident: ref_107 article-title: Complement drives glucosylceramide accumulation and tissue inflammation in Gaucher disease publication-title: Nature doi: 10.1038/nature21368 contributor: fullname: Pandey – volume: 13 start-page: 3355 year: 2002 ident: ref_115 article-title: Role of LAMP-2 in Lysosome Biogenesis and Autophagy publication-title: Mol. Biol. Cell doi: 10.1091/mbc.e02-02-0114 contributor: fullname: Eskelinen – volume: 1793 start-page: 684 year: 2009 ident: ref_7 article-title: Lysosomal disorders: From storage to cellular damage publication-title: Biochim. Biophys. Acta BBA-Mol. Cell Res. doi: 10.1016/j.bbamcr.2008.12.001 contributor: fullname: Ballabio – volume: 16 start-page: 4231 year: 2005 ident: ref_38 article-title: Role of the Endocytic Machinery in the Sorting of Lysosome-associated Membrane Proteins publication-title: Mol. Biol. Cell doi: 10.1091/mbc.e05-03-0213 contributor: fullname: Janvier – volume: 18 start-page: 923 year: 2019 ident: ref_80 article-title: Lysosomes as a therapeutic target publication-title: Nat. Rev. Drug Discov. doi: 10.1038/s41573-019-0036-1 contributor: fullname: Bonam – volume: 32 start-page: 1232 year: 2011 ident: ref_102 article-title: A mutation in SCARB2 is a modifier in gaucher disease publication-title: Hum. Mutat. doi: 10.1002/humu.21566 contributor: fullname: Velayati – volume: 129 start-page: 178 year: 2005 ident: ref_135 article-title: Gaucher disease: Pathological mechanisms and modern management publication-title: Br. J. Haematol. doi: 10.1111/j.1365-2141.2004.05351.x contributor: fullname: Jmoudiak – volume: 2 start-page: 232640981351766 year: 2014 ident: ref_5 article-title: Lysosomal Storage Diseases publication-title: J. Inborn Errors Metab. Screen. doi: 10.1177/2326409813517663 contributor: fullname: Alroy – volume: 377 start-page: 1290 year: 2022 ident: ref_52 article-title: Lysosomal GPCR-like protein LYCHOS signals cholesterol sufficiency to mTORC1 publication-title: Science doi: 10.1126/science.abg6621 contributor: fullname: Shin – volume: 7 start-page: 1574 year: 2015 ident: ref_79 article-title: The altered autophagy mediated by TFEB in animal and cell models of amyotrophic lateral sclerosis publication-title: Am. J. Transl. Res. contributor: fullname: Chen – volume: 21 start-page: 81 year: 2005 ident: ref_9 article-title: Principles of lysosomal membrane digestion: Stimulation of Sphingolipid Degradation by Sphingolipid Activator Proteins and Anionic Lysosomal Lipids publication-title: Annu. Rev. Cell Dev. Biol. doi: 10.1146/annurev.cellbio.21.122303.120013 contributor: fullname: Kolter – volume: 16 start-page: 611 year: 2019 ident: ref_85 article-title: Preserving Lysosomal Function in the Aging Brain: Insights from Neurodegeneration publication-title: Neurotherapeutics doi: 10.1007/s13311-019-00742-3 contributor: fullname: Peng – volume: 63 start-page: 103166 year: 2021 ident: ref_94 article-title: Impaired autophagy: The collateral damage of lysosomal storage disorders publication-title: EBioMedicine doi: 10.1016/j.ebiom.2020.103166 contributor: fullname: Myerowitz – volume: 26 start-page: 118 year: 2000 ident: ref_64 article-title: Identification of the gene causing mucolipidosis type IV publication-title: Nat. Genet. doi: 10.1038/79095 contributor: fullname: Bargal – ident: ref_78 doi: 10.3390/cells10020333 – volume: 4 start-page: 27 year: 2018 ident: ref_3 article-title: Lysosomal storage diseases publication-title: Nat. Rev. Dis. Primer doi: 10.1038/s41572-018-0025-4 contributor: fullname: Platt – volume: 77 start-page: 57 year: 2015 ident: ref_2 article-title: Lysosomal Physiology publication-title: Annu. Rev. Physiol. doi: 10.1146/annurev-physiol-021014-071649 contributor: fullname: Xu – volume: 129 start-page: 391 year: 2015 ident: ref_120 article-title: Danon disease: A phenotypic expression of LAMP-2 deficiency publication-title: Acta Neuropathol. doi: 10.1007/s00401-015-1385-4 contributor: fullname: Endo – ident: ref_109 – volume: 137 start-page: 1161 year: 1997 ident: ref_113 article-title: Different Steady State Subcellular Distributions of the Three Splice Variants of Lysosome-associated Membrane Protein LAMP-2 Are Determined Largely by the COOH-terminal Amino Acid Residue publication-title: J. Cell Biol. doi: 10.1083/jcb.137.5.1161 contributor: fullname: Gough – volume: 5 start-page: 11 year: 2001 ident: ref_41 article-title: Lysosomal membrane proteins publication-title: Eur. J. Paediatr. Neurol. doi: 10.1053/ejpn.2000.0428 contributor: fullname: Winchester – volume: 113 start-page: 435 year: 2003 ident: ref_133 article-title: Multiple Sulfatase Deficiency Is Caused by Mutations in the Gene Encoding the Human Cα-Formylglycine Generating Enzyme publication-title: Cell doi: 10.1016/S0092-8674(03)00347-7 contributor: fullname: Dierks – volume: 163 start-page: 755 year: 2003 ident: ref_18 article-title: Mammalian GGAs act together to sort mannose 6-phosphate receptors publication-title: J. Cell Biol. doi: 10.1083/jcb.200308038 contributor: fullname: Ghosh – volume: 18 start-page: 122 year: 2020 ident: ref_28 article-title: Focus on the morphogenesis, fate and the role in tumor progression of multivesicular bodies publication-title: Cell Commun. Signal. doi: 10.1186/s12964-020-00619-5 contributor: fullname: Peng – volume: 1793 start-page: 710 year: 2009 ident: ref_131 article-title: Molecular basis of multiple sulfatase deficiency, mucolipidosis II/III and Niemann–Pick C1 disease—Lysosomal storage disorders caused by defects of non-lysosomal proteins publication-title: Biochim. Biophys. Acta BBA Mol. Cell Res. doi: 10.1016/j.bbamcr.2008.11.015 contributor: fullname: Dierks – volume: 7 start-page: 12109 year: 2016 ident: ref_61 article-title: MCOLN1 is a ROS sensor in lysosomes that regulates autophagy publication-title: Nat. Commun. doi: 10.1038/ncomms12109 contributor: fullname: Zhang – ident: ref_126 doi: 10.1007/978-3-642-74415-0 – volume: 199 start-page: 723 year: 2012 ident: ref_93 article-title: Lysosomal storage disorders: The cellular impact of lysosomal dysfunction publication-title: J. Cell Biol. doi: 10.1083/jcb.201208152 contributor: fullname: Platt – volume: 10 start-page: 131 year: 2020 ident: ref_83 article-title: The role of lysosomes in cancer development and progression publication-title: Cell Biosci. doi: 10.1186/s13578-020-00489-x contributor: fullname: Tang – volume: 9 start-page: 583 year: 2013 ident: ref_6 article-title: Lysosomal storage diseases—the horizon expands publication-title: Nat. Rev. Neurol. doi: 10.1038/nrneurol.2013.163 contributor: fullname: Boustany – volume: 550 start-page: 415 year: 2017 ident: ref_63 article-title: Structure of mammalian endolysosomal TRPML1 channel in nanodiscs publication-title: Nature doi: 10.1038/nature24035 contributor: fullname: Chen – volume: 25 start-page: 1641 year: 2021 ident: ref_74 article-title: The important role of TFEB in autophagy-lysosomal pathway and autophagy-related diseases: A systematic review publication-title: Eur. Rev. Med. Pharmacol. Sci. contributor: fullname: Song – ident: ref_86 doi: 10.1371/journal.pone.0182895 – volume: 314 start-page: 306 year: 2004 ident: ref_33 article-title: Analysis of post-lysosomal compartments publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2003.12.092 contributor: fullname: Hirota – volume: 17 start-page: 133 year: 2018 ident: ref_92 article-title: Emptying the stores: Lysosomal diseases and therapeutic strategies publication-title: Nat. Rev. Drug Discov. doi: 10.1038/nrd.2017.214 contributor: fullname: Platt – volume: 406 start-page: 906 year: 2000 ident: ref_119 article-title: Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease) publication-title: Nature doi: 10.1038/35022604 contributor: fullname: Nishino – ident: ref_53 doi: 10.3390/biom7030051 – volume: 584 start-page: 2013 year: 2010 ident: ref_123 article-title: Mucolipins: Intracellular TRPML1-3 channels publication-title: FEBS Lett. doi: 10.1016/j.febslet.2009.12.056 contributor: fullname: Cheng – volume: 325 start-page: 473 year: 2009 ident: ref_75 article-title: A Gene Network Regulating Lysosomal Biogenesis and Function publication-title: Science doi: 10.1126/science.1174447 contributor: fullname: Sardiello – volume: 270 start-page: 27311 year: 1995 ident: ref_21 article-title: The Two Mannose 6-Phosphate Receptors Transport Distinct Complements of Lysosomal Proteins publication-title: J. Biol. Chem. doi: 10.1074/jbc.270.45.27311 contributor: fullname: Pohlmann – volume: 18 start-page: 221 year: 1965 ident: ref_134 article-title: Metabolism of glucocerebrosides II. Evidence of an enzymatic deficiency in Gaucher’s disease publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/0006-291X(65)90743-6 contributor: fullname: Brady – volume: 18 start-page: 1527 year: 2019 ident: ref_117 article-title: Danon disease: Two patients with atrial fibrillation in a single family and review of the literature publication-title: Exp. Ther. Med. contributor: fullname: Guo – volume: 396 start-page: 575 year: 1998 ident: ref_122 article-title: Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion publication-title: Nature doi: 10.1038/25133 contributor: fullname: Peters – ident: ref_90 doi: 10.1126/stke.2722005re3 – volume: 241 start-page: 1098 year: 1988 ident: ref_99 article-title: Coding of Two Sphingolipid Activator Proteins (SAP-1 and SAP-2) by Same Genetic Locus publication-title: Science doi: 10.1126/science.2842863 contributor: fullname: Kretz – volume: 82 start-page: 271 year: 1995 ident: ref_132 article-title: von A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency publication-title: Cell doi: 10.1016/0092-8674(95)90314-3 contributor: fullname: Schmidt – volume: 14 start-page: 273 year: 2012 ident: ref_108 article-title: Gaucher Disease: Insights from a Rare Mendelian Disorder publication-title: Discov. Med. contributor: fullname: Sidransky – volume: 14 start-page: 283 year: 2013 ident: ref_10 article-title: Signals from the lysosome: A control centre for cellular clearance and energy metabolism publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm3565 contributor: fullname: Settembre – volume: 332 start-page: 1429 year: 2011 ident: ref_12 article-title: TFEB Links Autophagy to Lysosomal Biogenesis publication-title: Science doi: 10.1126/science.1204592 contributor: fullname: Settembre – volume: Volume 362 start-page: 141 year: 2021 ident: ref_60 article-title: Lysosomal calcium and autophagy publication-title: International Review of Cell and Molecular Biology doi: 10.1016/bs.ircmb.2021.03.002 contributor: fullname: Medina – volume: 215 start-page: 757 year: 1995 ident: ref_121 article-title: An Alternatively Spliced Form of the Human Lysosome-Associated Membrane Protein-2 Gene Is Expressed in a Tissue-Specific Manner publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1995.2528 contributor: fullname: Konecki – volume: 95 start-page: 6373 year: 1998 ident: ref_140 article-title: Abnormal transport along the lysosomal pathway in Mucolipidosis, type IV disease publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.95.11.6373 contributor: fullname: Chen – volume: 129 start-page: 2135 year: 2016 ident: ref_137 article-title: Danon disease—dysregulation of autophagy in a multisystem disorder with cardiomyopathy publication-title: J. Cell Sci. doi: 10.1242/jcs.184770 contributor: fullname: Rowland – volume: 7 start-page: 568 year: 2006 ident: ref_24 article-title: Retrograde transport from endosomes to the trans-Golgi network publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm1985 contributor: fullname: Bonifacino – volume: 89 start-page: 862 year: 2016 ident: ref_72 article-title: Activation of the transcription factor EB rescues lysosomal abnormalities in cystinotic kidney cells publication-title: Kidney Int. doi: 10.1016/j.kint.2015.12.045 contributor: fullname: Rega – volume: 13 start-page: 7 year: 2019 ident: ref_100 article-title: Gaucher Disease: New Expanded Classification Emphasizing Neurological Features publication-title: Iran J Child Neurol contributor: fullname: Alaei – volume: 465 start-page: 942 year: 2010 ident: ref_36 article-title: Termination of autophagy and reformation of lysosomes regulated by mTOR publication-title: Nature doi: 10.1038/nature09076 contributor: fullname: Yu – volume: 8 start-page: 609683 year: 2021 ident: ref_73 article-title: MiT/TFE Family of Transcription Factors: An Evolutionary Perspective publication-title: Front. Cell Dev. Biol. doi: 10.3389/fcell.2020.609683 contributor: fullname: Contreras – volume: 9 start-page: 574 year: 2008 ident: ref_35 article-title: The Itinerary of Autophagosomes: From Peripheral Formation to Kiss-and-Run Fusion with Lysosomes publication-title: Traffic doi: 10.1111/j.1600-0854.2008.00701.x contributor: fullname: Jahreiss – volume: 148 start-page: 669 year: 2019 ident: ref_65 article-title: Current concepts in the neuropathogenesis of mucolipidosis type IV publication-title: J. Neurochem. doi: 10.1111/jnc.14462 contributor: fullname: Boudewyn – volume: 6 start-page: a016840 year: 2014 ident: ref_31 article-title: The Biogenesis of Lysosomes and Lysosome-Related Organelles publication-title: Cold Spring Harb. Perspect. Biol. doi: 10.1101/cshperspect.a016840 contributor: fullname: Luzio – volume: 30 start-page: 255 year: 2014 ident: ref_25 article-title: Biogenesis, Secretion, and Intercellular Interactions of Exosomes and Other Extracellular Vesicles publication-title: Annu. Rev. Cell Dev. Biol. doi: 10.1146/annurev-cellbio-101512-122326 contributor: fullname: Colombo – volume: 439 start-page: 349 year: 2011 ident: ref_57 article-title: Molecular mechanisms of endolysosomal Ca2+ signalling in health and disease publication-title: Biochem. J. doi: 10.1042/BJ20110949 contributor: fullname: Morgan – volume: 31 start-page: 51 year: 1981 ident: ref_89 article-title: Lysosomal glycogen storage disease with normal acid maltase publication-title: Neurology doi: 10.1212/WNL.31.1.51 contributor: fullname: Danon – volume: 8 start-page: 622 year: 2007 ident: ref_23 article-title: Lysosomes: Fusion and function publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm2217 contributor: fullname: Luzio – volume: 1 start-page: 38 year: 2010 ident: ref_62 article-title: PI(3,5)P2 controls membrane trafficking by direct activation of mucolipin Ca2+ release channels in the endolysosome publication-title: Nat. Commun. doi: 10.1038/ncomms1037 contributor: fullname: Dong – volume: 204 start-page: 115229 year: 2022 ident: ref_138 article-title: Autophagy guided interventions to modify the cardiac phenotype of Danon disease publication-title: Biochem. Pharmacol. doi: 10.1016/j.bcp.2022.115229 contributor: fullname: Yadin – volume: 285 start-page: 20423 year: 2010 ident: ref_8 article-title: Common and Uncommon Pathogenic Cascades in Lysosomal Storage Diseases publication-title: J. Biol. Chem. doi: 10.1074/jbc.R110.134452 contributor: fullname: Vitner – volume: 16 start-page: 70 year: 2009 ident: ref_27 article-title: Autophagy and multivesicular bodies: Two closely related partners publication-title: Cell Death Differ. doi: 10.1038/cdd.2008.168 contributor: fullname: Fader – volume: 04 start-page: 184 year: 2017 ident: ref_124 article-title: GM2 activator protein deficiency, mimic of Tay-Sachs disease publication-title: Int. J. Epilepsy doi: 10.1016/j.ijep.2017.08.001 contributor: fullname: Kochumon – ident: ref_125 – ident: ref_130 – volume: 4 start-page: 51 year: 2016 ident: ref_88 article-title: The ALS/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to regulate the autophagy-lysosome pathway publication-title: Acta Neuropathol. Commun. doi: 10.1186/s40478-016-0324-5 contributor: fullname: Sullivan – volume: 41 start-page: 374 year: 2000 ident: ref_17 article-title: A comparative structural analysis of the ADF/Cofilin family publication-title: Proteins Struct. Funct. Genet. doi: 10.1002/1097-0134(20001115)41:3<374::AID-PROT90>3.0.CO;2-F contributor: fullname: Bowman – volume: 57 start-page: 407 year: 2012 ident: ref_111 article-title: Danon disease: Focusing on heart publication-title: J. Hum. Genet. doi: 10.1038/jhg.2012.72 contributor: fullname: Cheng – volume: 7 start-page: 1388 year: 2006 ident: ref_139 article-title: Mucolipin-1 Is a Lysosomal Membrane Protein Required for Intracellular Lactosylceramide Traffic publication-title: Traffic doi: 10.1111/j.1600-0854.2006.00475.x contributor: fullname: Pryor – volume: 17 start-page: 2238 year: 2008 ident: ref_103 article-title: A nonsense mutation in the LIMP-2 gene associated with progressive myoclonic epilepsy and nephrotic syndrome publication-title: Hum. Mol. Genet. doi: 10.1093/hmg/ddn124 contributor: fullname: Balreira – volume: 72 start-page: 395 year: 2003 ident: ref_37 article-title: Signals for Sorting of Transmembrane Proteins to Endosomes and Lysosomes publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.72.121801.161800 contributor: fullname: Bonifacino – volume: 169 start-page: 361 year: 2017 ident: ref_48 article-title: mTOR Signaling in Growth, Metabolism, and Disease publication-title: Cell doi: 10.1016/j.cell.2017.03.035 contributor: fullname: Saxton – volume: 132 start-page: jcs221739 year: 2019 ident: ref_47 article-title: Lysosomal storage disorders—challenges, concepts and avenues for therapy: Beyond rare diseases publication-title: J. Cell Sci. doi: 10.1242/jcs.221739 contributor: fullname: Marques – volume: 44 start-page: 1274 year: 2021 ident: ref_30 article-title: MicroRNA 21 Elicits a Pro-inflammatory Response in Macrophages, with Exosomes Functioning as Delivery Vehicles publication-title: Inflammation doi: 10.1007/s10753-021-01415-0 contributor: fullname: Madhyastha – volume: 15 start-page: 360 year: 2005 ident: ref_34 article-title: Endocytic Delivery to Lysosomes Mediated by Concurrent Fusion and Kissing Events in Living Cells publication-title: Curr. Biol. doi: 10.1016/j.cub.2005.01.049 contributor: fullname: Bright – volume: 27 start-page: 495 year: 2006 ident: ref_112 article-title: Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy publication-title: Mol. Aspects Med. doi: 10.1016/j.mam.2006.08.005 contributor: fullname: Eskelinen – volume: 479 start-page: 489 year: 2016 ident: ref_114 article-title: Lysosome-associated membrane proteins-1 and -2 (LAMP-1 and LAMP-2) assemble via distinct modes publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2016.09.093 contributor: fullname: Terasawa – volume: 13 start-page: 137 year: 2003 ident: ref_42 article-title: At the acidic edge: Emerging functions for lysosomal membrane proteins publication-title: Trends Cell Biol. doi: 10.1016/S0962-8924(03)00005-9 contributor: fullname: Eskelinen – volume: 10 start-page: 623 year: 2009 ident: ref_15 article-title: Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm2745 contributor: fullname: Saftig – volume: 21 start-page: 421 year: 2011 ident: ref_70 article-title: Transcriptional Activation of Lysosomal Exocytosis Promotes Cellular Clearance publication-title: Dev. Cell doi: 10.1016/j.devcel.2011.07.016 contributor: fullname: Medina – volume: 84 start-page: 275 year: 2014 ident: ref_81 article-title: The Neurology of mTOR publication-title: Neuron doi: 10.1016/j.neuron.2014.09.034 contributor: fullname: Lipton |
| SSID | ssj0000913814 |
| Score | 2.3409188 |
| SecondaryResourceType | review_article |
| Snippet | Since its discovery in 1955, the understanding of the lysosome has continuously increased. Once considered a mere waste removal system, the lysosome is now... |
| SourceID | doaj pubmedcentral proquest crossref pubmed |
| SourceType | Open Website Open Access Repository Aggregation Database Index Database |
| StartPage | 213 |
| SubjectTerms | Autophagy Biology Biosynthesis Disease endocytic pathway Endoplasmic reticulum Energy metabolism Enzymes Gene expression Genetic disorders lysosomal disease lysosome lysosome biogenesis and function Lysosomes Metabolism Plasma Proteins Review Signal transduction Transcription factors |
| SummonAdditionalLinks | – databaseName: Directory of Open Access Journals dbid: DOA link: http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV07T8MwED4BEwyIN-ElI7FG2PElTth4VQwIBkBii-zEFgwkqGkH_j1np61ahMTCGnu4fJfz3Rfb3wGcyUxZp7xyK6o6Ro1pbJLExkmq0WhrcsH9fee7J_Xwmt_cepmcWasvfyaslwfugTtHXkvK0blLsCYuYKgc1rlBnftWyehcWH25miNTYQ0uBKUi7O_KSeL15_1t9rBb3VHK8x2t5UIuCpL9v9WZP49LzuWfwQasTwpHdtkbvAlLttmCtTk5wW3g5HPWN5f8Yq1j919d25E93QUbDNsP9uhlNtmoZVPJzR14Gdw-X9_Fk44IcZVKPooxsSm3OkuNchRIBoVzXDmrXVpjRVxIK-G0RKJ1BXEFXRB9srUVBVbouJFyF1aatrH7wAhPwXVacaqoUDmpeWVMoXhlC5FzaSKIp9iUn73wRUmEwWNZ_oZlBFcewNlcL1sdHpAzy4kzy7-cGcHRFP5yEktdmaiMEijRRB7B6WyYosBvbejGtuMwhyqdPCvIjr3eWzNLZBZ2m0UEasGPC6YujjTvb0Fpu8ipIEzEwX-82yGs-lb1_veNwCNYGQ3H9hiWu3p8Er7db7eh8hc priority: 102 providerName: Directory of Open Access Journals |
| Title | The Biology of Lysosomes: From Order to Disorder |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/36672721 https://www.proquest.com/docview/2767182490 https://www.proquest.com/docview/2768228693 https://pubmed.ncbi.nlm.nih.gov/PMC9856021 https://doaj.org/article/40d35628f24d401b826a8b4a844084ff |
| Volume | 11 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT-MwEB5RTnBY8d4sDxlpr6F27MQJN14VB2CRAIlbZCc2IG0T1LQH_j1jJ6laxIlrnCiTGTsznz3zDcBfnkhjpWNuFbIMhRJxqKPIhFGshFZGp4y6eufrB3n3nF5eOZqcuK-F8Un7hX47qf6PT6q3V59b-T4uhn2e2PD-9iJL0U9HbDiAAcaGCxDd_34zhl5ItGVyHCH9sC1k9wfVDXo718zatc_hiT-FZEseyRP3fxdtfk2aXPBCow341YWP5KwVcxNWTLUF6wukgttA0fKkbTH5QWpLbj6aukHRmlMymtRj8s-RbZJpTXrizR14Gl09XlyHXV-EsIg5nYYiMjE1Kom1tLictGDWUmmNsnEpCkRESjKruMBvyxAxqAxBlCkNy0QhLNWc78JqVVfmNxCLDpyquKAYVwlpuaKF1pmkhclYSrkOIOx1k7-39Bc5wgan1vw7tQZw7hQ4v9eRV_sL9eQl70yYC1pyDLtSfHmJ8E4jwlGpFip13a-FtQEc9OrPuxXV5JFM0I0iWKQBHM-HcS24Aw5VmXrm78F4J00ylGOvtdZckt7aAcglOy6JujyC08_zbXfT7c-Pn9yHNdel3u3cMHEAq9PJzBzCoClnR34P4MjP4E_HK_SV |
| link.rule.ids | 230,315,729,782,786,866,887,2107,27934,27935,53802,53804 |
| linkProvider | National Library of Medicine |
| linkToHtml | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3fb9MwED6x8QB7AMZgBArzpL1mtWMnTniD0arTuh_SNmlvkZ3YMIkmU9M-7L_n7CRVi_a019hRnDtf7r747juAI55IY6VjbhWyDIUScaijyIRRrIRWRqeMunrnybW8uEt_jRxNTtzXwvik_ULfH1d_Z8fV_R-fW_kwK4Z9ntjw6vwkS9FPR2y4BS_RXmm0BtL9Bzhj6IdEWyjHEdQP21J2f1TdoL9z7axdAx2e-HNItuGTPHX_U_Hm_2mTa35o_PaZb_AO3nSBJ_nRDu_CC1O9h501OsI9oLhnSNuc8pHUlkwfm7rBV2q-k_G8npFLR9NJFjXpKTs_wO14dHMyCbuOCmERc7oIRWRialQSa2nRELVg1lJpjbJxKQrEUkoyq7hAmWSINVSG8MuUhmWiEJZqzj_CdlVX5hMQi66fqrigGJEJabmihdaZpIXJWEq5DiDsZZo_tMQZOQIOp478KXUE8NMJfjXX0V77C_X8d96JLhe05BiwpfjwEoGhRmykUi1U6vpmC2sDGPRqyztbbPJIJuiAEWbSAA5Xw2hF7mhEVaZe-jkYKaVJhuvYb7W8Wkm_SwKQG_rfWOrmCKrdM3V3av787DsP4NXk5nyaT08vzr7Aa9fr3v3_YWIA24v50nyFraZcfvP7_x_E6wk4 |
| linkToPdf | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Lb9QwEB7RIiE48H4EChiJaxo7nsQJN2i7KqKUSoDELbITGyqxyWqze-i_Z-wkq13UE1xjR7FnPJn57PE3AG9lrqxTnrkVVROjxiw2aWrjNNNotDWF4P6-8-lXdf6jOD7xNDmbUl8hab82l4ft7_lhe_kr5FYu5nUy5YklF5-PyoL8dCqSReOSPbhJNstxC6iHn3ApyBfhcFlOErBPhuvs4bi6J5_nS1r7IjoyD2eRYscvBfr-62LOv1Mnt3zR7N5_zOI-3B0DUPZ-6PIAbtj2IdzZoiV8BJzWDhuKVF6xzrGzq77raVr9OzZbdnP2xdN1slXHJurOx_B9dvLt6DQeKyvEdSb5KsbUZtzqPDPKkUEaFM5x5ax2WYM1YSqthNMSSS4lYQ5dEgyzjRUl1ui4kfIJ7Ldda58BcxQCcJ3VnCIzVE5qXhtTKl7bUhRcmgjiSa7VYiDQqAh4eJVU16kkgg9e-Ju-nv46POiWP6tRfBXyRlLgVtDHGwKIhjCSLgzqwtfPRuciOJhUV4022VepyskRE9zkEbzZNJM1-SMS3dpuHfpQxFTkJY3j6aDpzUimlRKB2lkDO0PdbSHVB8buUdXP__nN13Dr4nhWnX08__QCbvuS934bSOAB7K-Wa_sS9vpm_SqYwB8q_Qu4 |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=The+Biology+of+Lysosomes%3A+From+Order+to+Disorder&rft.jtitle=Biomedicines&rft.au=Amaral%2C+Olga&rft.au=Martins%2C+Mariana&rft.au=Oliveira%2C+Ana+Rita&rft.au=Duarte%2C+Ana+Joana&rft.date=2023-01-14&rft.issn=2227-9059&rft.eissn=2227-9059&rft.volume=11&rft.issue=1&rft_id=info:doi/10.3390%2Fbiomedicines11010213&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2227-9059&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2227-9059&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2227-9059&client=summon |