CARTS biogenesis requires VAP–lipid transfer protein complexes functioning at the endoplasmic reticulum–Golgi interface
Biogenesis of the TGN-derived transport carriers CARTS requires the ER protein VAP and Golgi lipid transfer proteins, ceramide transfer protein and OSBP. Sac1 lipid phosphatase is recruited to a VAP–OSBP complex formed at an ER subdomain closely apposed to the trans-Golgi/TGN. Association–dissociati...
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The American Society for Cell Biology
2015
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Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4678024/ |
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pubmed-46780242016-03-01 CARTS biogenesis requires VAP–lipid transfer protein complexes functioning at the endoplasmic reticulum–Golgi interface Wakana, Yuichi Kotake, Richika Oyama, Nanako Murate, Motohide Kobayashi, Toshihide Arasaki, Kohei Inoue, Hiroki Tagaya, Mitsuo Articles Biogenesis of the TGN-derived transport carriers CARTS requires the ER protein VAP and Golgi lipid transfer proteins, ceramide transfer protein and OSBP. Sac1 lipid phosphatase is recruited to a VAP–OSBP complex formed at an ER subdomain closely apposed to the trans-Golgi/TGN. Association–dissociation dynamics of ER–Golgi contacts are important for CARTS formation. The American Society for Cell Biology 2015-12-15 /pmc/articles/PMC4678024/ /pubmed/26490117 http://dx.doi.org/10.1091/mbc.E15-08-0599 Text en © 2015 Wakana 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. |
repository_type |
Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Wakana, Yuichi Kotake, Richika Oyama, Nanako Murate, Motohide Kobayashi, Toshihide Arasaki, Kohei Inoue, Hiroki Tagaya, Mitsuo |
spellingShingle |
Wakana, Yuichi Kotake, Richika Oyama, Nanako Murate, Motohide Kobayashi, Toshihide Arasaki, Kohei Inoue, Hiroki Tagaya, Mitsuo CARTS biogenesis requires VAP–lipid transfer protein complexes functioning at the endoplasmic reticulum–Golgi interface |
author_facet |
Wakana, Yuichi Kotake, Richika Oyama, Nanako Murate, Motohide Kobayashi, Toshihide Arasaki, Kohei Inoue, Hiroki Tagaya, Mitsuo |
author_sort |
Wakana, Yuichi |
title |
CARTS biogenesis requires VAP–lipid transfer protein complexes functioning at the endoplasmic reticulum–Golgi interface |
title_short |
CARTS biogenesis requires VAP–lipid transfer protein complexes functioning at the endoplasmic reticulum–Golgi interface |
title_full |
CARTS biogenesis requires VAP–lipid transfer protein complexes functioning at the endoplasmic reticulum–Golgi interface |
title_fullStr |
CARTS biogenesis requires VAP–lipid transfer protein complexes functioning at the endoplasmic reticulum–Golgi interface |
title_full_unstemmed |
CARTS biogenesis requires VAP–lipid transfer protein complexes functioning at the endoplasmic reticulum–Golgi interface |
title_sort |
carts biogenesis requires vap–lipid transfer protein complexes functioning at the endoplasmic reticulum–golgi interface |
description |
Biogenesis of the TGN-derived transport carriers CARTS requires the ER protein VAP and Golgi lipid transfer proteins, ceramide transfer protein and OSBP. Sac1 lipid phosphatase is recruited to a VAP–OSBP complex formed at an ER subdomain closely apposed to the trans-Golgi/TGN. Association–dissociation dynamics of ER–Golgi contacts are important for CARTS formation. |
publisher |
The American Society for Cell Biology |
publishDate |
2015 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4678024/ |
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1613512568204165120 |