期刊
MOLECULAR BIOLOGY OF THE CELL
卷 26, 期 25, 页码 4686-4699出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E15-08-0599
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资金
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [25291029, 25840042]
- NOVARTIS Foundation (Japan) for the Promotion of Science
- Uehara Memorial Foundation
- Grants-in-Aid for Scientific Research [26111520, 25840042, 26650066, 15K18507, 15K08167] Funding Source: KAKEN
Vesicle-associated membrane protein-associated protein (VAP) is an endoplasmic reticulum (ER)-resident integral membrane protein that controls a nonvesicular mode of ceramide and cholesterol transfer from the ER to the Golgi complex by interacting with ceramide transfer protein and oxysterol-binding protein (OSBP), respectively. We report that VAP and its interacting proteins are required for the processing and secretion of pancreatic adenocarcinoma up-regulated factor, whose transport from the trans-Golgi network (TGN) to the cell surface is mediated by transport carriers called carriers of the trans-Golgi network to the cell surface (CARTS). In VAP-depleted cells, diacylglycerol level at the TGN was decreased and CARTS formation was impaired. We found that VAP forms a complex with not only OSBP but also Sac1 phosphoinositide phosphatase at specialized ER subdomains that are closely apposed to the trans-Golgi/TGN, most likely reflecting membrane contact sites. Immobilization of ER-Golgi contacts dramatically reduced CARTS production, indicating that association-dissociation dynamics of the two membranes are important. On the basis of these findings, we propose that the ER-Golgi contacts play a pivotal role in lipid metabolism to control the biogenesis of transport carriers from the TGN.
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