Tau protein modifications and interactions: their role in function and dysfunction
Tau protein is abundant in the central nervous system and involved in microtubule assembly and stabilization. It is predominantly associated with axonal microtubules and present at lower level in dendrites where it is engaged in signaling functions. Post-translational modifications of tau and its in...
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| Published in: | International journal of molecular sciences Vol. 15; no. 3; pp. 4671 - 4713 |
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| Main Authors: | , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
Switzerland
MDPI AG
18-03-2014
Molecular Diversity Preservation International (MDPI) |
| Subjects: | |
| Online Access: | Get full text |
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| Abstract | Tau protein is abundant in the central nervous system and involved in microtubule assembly and stabilization. It is predominantly associated with axonal microtubules and present at lower level in dendrites where it is engaged in signaling functions. Post-translational modifications of tau and its interaction with several proteins play an important regulatory role in the physiology of tau. As a consequence of abnormal modifications and expression, tau is redistributed from neuronal processes to the soma and forms toxic oligomers or aggregated deposits. The accumulation of tau protein is increasingly recognized as the neuropathological hallmark of a number of dementia disorders known as tauopathies. Dysfunction of tau protein may contribute to collapse of cytoskeleton, thereby causing improper anterograde and retrograde movement of motor proteins and their cargos on microtubules. These disturbances in intraneuronal signaling may compromise synaptic transmission as well as trophic support mechanisms in neurons. |
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| AbstractList | Tau protein is abundant in the central nervous system and involved in microtubule assembly and stabilization. It is predominantly associated with axonal microtubules and present at lower level in dendrites where it is engaged in signaling functions. Post-translational modifications of tau and its interaction with several proteins play an important regulatory role in the physiology of tau. As a consequence of abnormal modifications and expression, tau is redistributed from neuronal processes to the soma and forms toxic oligomers or aggregated deposits. The accumulation of tau protein is increasingly recognized as the neuropathological hallmark of a number of dementia disorders known as tauopathies. Dysfunction of tau protein may contribute to collapse of cytoskeleton, thereby causing improper anterograde and retrograde movement of motor proteins and their cargos on microtubules. These disturbances in intraneuronal signaling may compromise synaptic transmission as well as trophic support mechanisms in neurons. |
| Author | Mietelska-Porowska, Anna Goras, Marcelina Niewiadomska, Grazyna Wasik, Urszula Filipek, Anna |
| Author_xml | – sequence: 1 givenname: Anna surname: Mietelska-Porowska fullname: Mietelska-Porowska, Anna email: a.mietelska@nencki.gov.pl organization: Nencki Institute of Experimental Biology, Polish Academy of Science, 3 Pasteur Street, Warsaw 02-093, Poland. a.mietelska@nencki.gov.pl – sequence: 2 givenname: Urszula surname: Wasik fullname: Wasik, Urszula email: uwasik@nencki.gov.pl organization: Nencki Institute of Experimental Biology, Polish Academy of Science, 3 Pasteur Street, Warsaw 02-093, Poland. uwasik@nencki.gov.pl – sequence: 3 givenname: Marcelina surname: Goras fullname: Goras, Marcelina email: m.goras@nencki.gov.pl organization: Nencki Institute of Experimental Biology, Polish Academy of Science, 3 Pasteur Street, Warsaw 02-093, Poland. m.goras@nencki.gov.pl – sequence: 4 givenname: Anna surname: Filipek fullname: Filipek, Anna email: a.filipek@nencki.gov.pl organization: Nencki Institute of Experimental Biology, Polish Academy of Science, 3 Pasteur Street, Warsaw 02-093, Poland. a.filipek@nencki.gov.pl – sequence: 5 givenname: Grazyna surname: Niewiadomska fullname: Niewiadomska, Grazyna email: g.niewiadomska@nencki.gov.pl organization: Nencki Institute of Experimental Biology, Polish Academy of Science, 3 Pasteur Street, Warsaw 02-093, Poland. g.niewiadomska@nencki.gov.pl |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24646911$$D View this record in MEDLINE/PubMed |
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