Nucleotide bound to rab11a controls localization in rod cells but not interaction with rhodopsin
Precise vectorial transport of rhodopsin is essential for rod photoreceptor health and function. Mutations that truncate or extend the C terminus of rhodopsin disrupt this transport, and lead to retinal degeneration and blindness in human patients and in mouse models. Here we show that such mutation...
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| Published in: | The Journal of neuroscience Vol. 34; no. 45; pp. 14854 - 14863 |
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05-11-2014
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| Abstract | Precise vectorial transport of rhodopsin is essential for rod photoreceptor health and function. Mutations that truncate or extend the C terminus of rhodopsin disrupt this transport, and lead to retinal degeneration and blindness in human patients and in mouse models. Here we show that such mutations disrupt the binding of rhodopsin to the small GTPase rab11a. The rhodopsin-rab11a interaction is a direct binding interaction that does not depend on the nucleotide binding state of rab11a. Expression of EGFP-rab11a fusion proteins in Xenopus laevis photoreceptors revealed that the nucleotide binding status of rab11a affects its subcellular localization, with GTP-locked mutants concentrated in the inner segment and GDP-locked mutants concentrated in the outer segment. shRNA-mediated knockdown of rab11a in rods led to shortened outer segments and retinal degeneration. Together, our results show the critical importance of direct rhodopsin-rab11a interactions for the formation and maintenance of vertebrate photoreceptors. |
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| AbstractList | Precise vectorial transport of rhodopsin is essential for rod photoreceptor health and function. Mutations that truncate or extend the C terminus of rhodopsin disrupt this transport, and lead to retinal degeneration and blindness in human patients and in mouse models. Here we show that such mutations disrupt the binding of rhodopsin to the small GTPase rab11a. The rhodopsin-rab11a interaction is a direct binding interaction that does not depend on the nucleotide binding state of rab11a. Expression of EGFP-rab11a fusion proteins in Xenopus laevis photoreceptors revealed that the nucleotide binding status of rab11a affects its subcellular localization, with GTP-locked mutants concentrated in the inner segment and GDP-locked mutants concentrated in the outer segment. shRNA-mediated knockdown of rab11a in rods led to shortened outer segments and retinal degeneration. Together, our results show the critical importance of direct rhodopsin-rab11a interactions for the formation and maintenance of vertebrate photoreceptors. Precise vectorial transport of rhodopsin is essential for rod photoreceptor health and function. Mutations that truncate or extend the C terminus of rhodopsin disrupt this transport, and lead to retinal degeneration and blindness in human patients and in mouse models. Here we show that such mutations disrupt the binding of rhodopsin to the small GTPase rab11a. The rhodopsin–rab11a interaction is a direct binding interaction that does not depend on the nucleotide binding state of rab11a. Expression of EGFP-rab11a fusion proteins in Xenopus laevis photoreceptors revealed that the nucleotide binding status of rab11a affects its subcellular localization, with GTP-locked mutants concentrated in the inner segment and GDP-locked mutants concentrated in the outer segment. shRNA-mediated knockdown of rab11a in rods led to shortened outer segments and retinal degeneration. Together, our results show the critical importance of direct rhodopsin–rab11a interactions for the formation and maintenance of vertebrate photoreceptors. |
| Author | Bales, Katie L Gross, Alecia K Boitet, Evan R Reish, Nicholas J |
| Author_xml | – sequence: 1 givenname: Nicholas J surname: Reish fullname: Reish, Nicholas J organization: Evelyn F. McKnight Brain Institute, Department of Neurobiology, and – sequence: 2 givenname: Evan R surname: Boitet fullname: Boitet, Evan R organization: Evelyn F. McKnight Brain Institute, Department of Vision Sciences, School of Optometry, University of Alabama at Birmingham, Birmingham, Alabama 35294 – sequence: 3 givenname: Katie L surname: Bales fullname: Bales, Katie L organization: Evelyn F. McKnight Brain Institute, Department of Vision Sciences, School of Optometry, University of Alabama at Birmingham, Birmingham, Alabama 35294 – sequence: 4 givenname: Alecia K orcidid: 0000-0003-1857-6633 surname: Gross fullname: Gross, Alecia K email: agross@uab.edu organization: Evelyn F. McKnight Brain Institute, Department of Neurobiology, and Department of Vision Sciences, School of Optometry, University of Alabama at Birmingham, Birmingham, Alabama 35294 agross@uab.edu |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25378153$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1371_journal_pone_0161236 crossref_primary_10_1021_acs_biochem_5b00003 crossref_primary_10_1096_fj_201801740RR crossref_primary_10_3389_fcell_2020_603794 crossref_primary_10_1146_annurev_vision_091718_014843 crossref_primary_10_1007_s12017_018_8479_9 crossref_primary_10_1016_j_preteyeres_2017_05_001 crossref_primary_10_1016_j_exer_2015_11_007 crossref_primary_10_1242_jcs_175687 crossref_primary_10_1080_21541248_2015_1091539 crossref_primary_10_1371_journal_pbio_3002467 |
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| Issue | 45 |
| Keywords | protein interactions rhodopsin rab11a protein trafficking |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Author contributions: N.J.R. and A.K.G. designed research; N.J.R., E.R.B., K.L.B., and A.K.G. performed research; A.K.G. contributed unpublished reagents/analytic tools; N.J.R., E.R.B., K.L.B., and A.K.G. analyzed data; N.J.R., E.R.B., K.L.B., and A.K.G. wrote the paper. |
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| Snippet | Precise vectorial transport of rhodopsin is essential for rod photoreceptor health and function. Mutations that truncate or extend the C terminus of rhodopsin... |
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| SubjectTerms | Animals Binding Sites Guanosine Triphosphate - metabolism Mice Mutation Protein Binding Protein Transport rab GTP-Binding Proteins - chemistry rab GTP-Binding Proteins - genetics rab GTP-Binding Proteins - metabolism Rhodopsin - metabolism Rod Cell Outer Segment - metabolism Xenopus Xenopus laevis |
| Title | Nucleotide bound to rab11a controls localization in rod cells but not interaction with rhodopsin |
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