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Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic
Yeast Vps13 is a member of a conserved protein family that includes human homologues associated with neurodegenerative and developmental disorders. In this issue, De et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201606078) establish direct roles for Vps13 and its surprising binding partner...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Rockefeller University Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5294792/ https://www.ncbi.nlm.nih.gov/pubmed/28122956 http://dx.doi.org/10.1083/jcb.201612026 |
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author | Myers, Margaret D. Payne, Gregory S. |
author_facet | Myers, Margaret D. Payne, Gregory S. |
author_sort | Myers, Margaret D. |
collection | PubMed |
description | Yeast Vps13 is a member of a conserved protein family that includes human homologues associated with neurodegenerative and developmental disorders. In this issue, De et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201606078) establish direct roles for Vps13 and its surprising binding partner, the calcium-binding centrin Cdc31, in trans-Golgi network (TGN) to endosome traffic and TGN homotypic fusion. |
format | Online Article Text |
id | pubmed-5294792 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-52947922017-08-01 Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic Myers, Margaret D. Payne, Gregory S. J Cell Biol Commentary Yeast Vps13 is a member of a conserved protein family that includes human homologues associated with neurodegenerative and developmental disorders. In this issue, De et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201606078) establish direct roles for Vps13 and its surprising binding partner, the calcium-binding centrin Cdc31, in trans-Golgi network (TGN) to endosome traffic and TGN homotypic fusion. The Rockefeller University Press 2017-02 /pmc/articles/PMC5294792/ /pubmed/28122956 http://dx.doi.org/10.1083/jcb.201612026 Text en © 2017 Myers and Payne http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Commentary Myers, Margaret D. Payne, Gregory S. Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic |
title | Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic |
title_full | Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic |
title_fullStr | Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic |
title_full_unstemmed | Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic |
title_short | Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic |
title_sort | vps13 and cdc31/centrin: puzzling partners in membrane traffic |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5294792/ https://www.ncbi.nlm.nih.gov/pubmed/28122956 http://dx.doi.org/10.1083/jcb.201612026 |
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