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Transport vesicle uncoating: it’s later than you think
Transport vesicle coat proteins play active roles in vesicle cargo sorting as well as membrane deformation and fission during vesicle biogenesis. For years, it was assumed that this was the extent of the coats’ function and that the coats depolymerized immediately after vesicle budding, leaving the...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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Faculty of 1000 Ltd
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2919759/ https://www.ncbi.nlm.nih.gov/pubmed/20706600 http://dx.doi.org/10.3410/B2-47 |
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author | Trahey, Meg Hay, Jesse C |
author_facet | Trahey, Meg Hay, Jesse C |
author_sort | Trahey, Meg |
collection | PubMed |
description | Transport vesicle coat proteins play active roles in vesicle cargo sorting as well as membrane deformation and fission during vesicle biogenesis. For years, it was assumed that this was the extent of the coats’ function and that the coats depolymerized immediately after vesicle budding, leaving the exposed fusion machinery free to find, dock, and fuse with the proper target membrane. Recently, however, it has become increasingly clear that the coat remains on transport vesicles during their post-budding life and in fact helps properly pair up the vesicle with its intended target membrane. These data have brought up urgent questions about exactly when vesicles do uncoat and how uncoating is regulated. Here, we summarize the latest round of evidence for post-budding roles for coats, including a few hints about how the uncoating process may be coupled to docking and fusion. We also speculate about the possibility of post-fusion functions for residual coats. |
format | Text |
id | pubmed-2919759 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Faculty of 1000 Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-29197592010-08-11 Transport vesicle uncoating: it’s later than you think Trahey, Meg Hay, Jesse C F1000 Biol Rep Review Article Transport vesicle coat proteins play active roles in vesicle cargo sorting as well as membrane deformation and fission during vesicle biogenesis. For years, it was assumed that this was the extent of the coats’ function and that the coats depolymerized immediately after vesicle budding, leaving the exposed fusion machinery free to find, dock, and fuse with the proper target membrane. Recently, however, it has become increasingly clear that the coat remains on transport vesicles during their post-budding life and in fact helps properly pair up the vesicle with its intended target membrane. These data have brought up urgent questions about exactly when vesicles do uncoat and how uncoating is regulated. Here, we summarize the latest round of evidence for post-budding roles for coats, including a few hints about how the uncoating process may be coupled to docking and fusion. We also speculate about the possibility of post-fusion functions for residual coats. Faculty of 1000 Ltd 2010-06-23 /pmc/articles/PMC2919759/ /pubmed/20706600 http://dx.doi.org/10.3410/B2-47 Text en © 2010 Faculty of 1000 Ltd http://creativecommons.org/licenses/by-nc/3.0/legalcode This is an open-access article distributed under the terms of the Creative Commons Attribution-Non Commercial License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. You may not use this work for commercial purposes |
spellingShingle | Review Article Trahey, Meg Hay, Jesse C Transport vesicle uncoating: it’s later than you think |
title | Transport vesicle uncoating: it’s later than you think |
title_full | Transport vesicle uncoating: it’s later than you think |
title_fullStr | Transport vesicle uncoating: it’s later than you think |
title_full_unstemmed | Transport vesicle uncoating: it’s later than you think |
title_short | Transport vesicle uncoating: it’s later than you think |
title_sort | transport vesicle uncoating: it’s later than you think |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2919759/ https://www.ncbi.nlm.nih.gov/pubmed/20706600 http://dx.doi.org/10.3410/B2-47 |
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