Cargando…
Auxilin facilitates membrane traffic in the early secretory pathway
Coat protein complexes contain an inner shell that sorts cargo and an outer shell that helps deform the membrane to give the vesicle its shape. There are three major types of coated vesicles in the cell: COPII, COPI, and clathrin. The COPII coat complex facilitates vesicle budding from the endoplasm...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4694752/ https://www.ncbi.nlm.nih.gov/pubmed/26538028 http://dx.doi.org/10.1091/mbc.E15-09-0631 |
_version_ | 1782407514339409920 |
---|---|
author | Ding, Jingzhen Segarra, Verónica A. Chen, Shuliang Cai, Huaqing Lemmon, Sandra K. Ferro-Novick, Susan |
author_facet | Ding, Jingzhen Segarra, Verónica A. Chen, Shuliang Cai, Huaqing Lemmon, Sandra K. Ferro-Novick, Susan |
author_sort | Ding, Jingzhen |
collection | PubMed |
description | Coat protein complexes contain an inner shell that sorts cargo and an outer shell that helps deform the membrane to give the vesicle its shape. There are three major types of coated vesicles in the cell: COPII, COPI, and clathrin. The COPII coat complex facilitates vesicle budding from the endoplasmic reticulum (ER), while the COPI coat complex performs an analogous function in the Golgi. Clathrin-coated vesicles mediate traffic from the cell surface and between the trans-Golgi and endosome. While the assembly and structure of these coat complexes has been extensively studied, the disassembly of COPII and COPI coats from membranes is less well understood. We describe a proteomic and genetic approach that connects the J-domain chaperone auxilin, which uncoats clathrin-coated vesicles, to COPII and COPI coat complexes. Consistent with a functional role for auxilin in the early secretory pathway, auxilin binds to COPII and COPI coat subunits. Furthermore, ER–Golgi and intra-Golgi traffic is delayed at 15°C in swa2Δ mutant cells, which lack auxilin. In the case of COPII vesicles, we link this delay to a defect in vesicle fusion. We propose that auxilin acts as a chaperone and/or uncoating factor for transport vesicles that act in the early secretory pathway. |
format | Online Article Text |
id | pubmed-4694752 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-46947522016-03-16 Auxilin facilitates membrane traffic in the early secretory pathway Ding, Jingzhen Segarra, Verónica A. Chen, Shuliang Cai, Huaqing Lemmon, Sandra K. Ferro-Novick, Susan Mol Biol Cell Articles Coat protein complexes contain an inner shell that sorts cargo and an outer shell that helps deform the membrane to give the vesicle its shape. There are three major types of coated vesicles in the cell: COPII, COPI, and clathrin. The COPII coat complex facilitates vesicle budding from the endoplasmic reticulum (ER), while the COPI coat complex performs an analogous function in the Golgi. Clathrin-coated vesicles mediate traffic from the cell surface and between the trans-Golgi and endosome. While the assembly and structure of these coat complexes has been extensively studied, the disassembly of COPII and COPI coats from membranes is less well understood. We describe a proteomic and genetic approach that connects the J-domain chaperone auxilin, which uncoats clathrin-coated vesicles, to COPII and COPI coat complexes. Consistent with a functional role for auxilin in the early secretory pathway, auxilin binds to COPII and COPI coat subunits. Furthermore, ER–Golgi and intra-Golgi traffic is delayed at 15°C in swa2Δ mutant cells, which lack auxilin. In the case of COPII vesicles, we link this delay to a defect in vesicle fusion. We propose that auxilin acts as a chaperone and/or uncoating factor for transport vesicles that act in the early secretory pathway. The American Society for Cell Biology 2016-01-01 /pmc/articles/PMC4694752/ /pubmed/26538028 http://dx.doi.org/10.1091/mbc.E15-09-0631 Text en © 2016 Ding, Segarra, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Ding, Jingzhen Segarra, Verónica A. Chen, Shuliang Cai, Huaqing Lemmon, Sandra K. Ferro-Novick, Susan Auxilin facilitates membrane traffic in the early secretory pathway |
title | Auxilin facilitates membrane traffic in the early secretory pathway |
title_full | Auxilin facilitates membrane traffic in the early secretory pathway |
title_fullStr | Auxilin facilitates membrane traffic in the early secretory pathway |
title_full_unstemmed | Auxilin facilitates membrane traffic in the early secretory pathway |
title_short | Auxilin facilitates membrane traffic in the early secretory pathway |
title_sort | auxilin facilitates membrane traffic in the early secretory pathway |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4694752/ https://www.ncbi.nlm.nih.gov/pubmed/26538028 http://dx.doi.org/10.1091/mbc.E15-09-0631 |
work_keys_str_mv | AT dingjingzhen auxilinfacilitatesmembranetrafficintheearlysecretorypathway AT segarraveronicaa auxilinfacilitatesmembranetrafficintheearlysecretorypathway AT chenshuliang auxilinfacilitatesmembranetrafficintheearlysecretorypathway AT caihuaqing auxilinfacilitatesmembranetrafficintheearlysecretorypathway AT lemmonsandrak auxilinfacilitatesmembranetrafficintheearlysecretorypathway AT ferronovicksusan auxilinfacilitatesmembranetrafficintheearlysecretorypathway |