期刊
JOURNAL OF CELL BIOLOGY
卷 217, 期 6, 页码 2073-2085出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201708115
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资金
- National Institutes of Health Office of Research Infrastructure Programs [P40 OD010440]
- Japan Society for the Promotion of Science KAKENHI [26291036, 17K19377, 17H03669]
- Uehara Memorial Foundation
- Ono Medical Research Foundation
- Takeda Science Foundation
- Ministry of Education, Culture, Sports, Science and Technology KAKENHI [16H01191]
- Joint Research Program of the Institute for Molecular and Cellular Regulation at Gunma University
- [16J11698]
- Grants-in-Aid for Scientific Research [26291036, 17H03669, 17K19377, 16H01191, 16J11698] Funding Source: KAKEN
Lipoproteins regulate the overall lipid homeostasis in animals. However, the molecular mechanisms underlying lipoprotein trafficking remain poorly understood. Here, we show that SFT-4, a Caenorhabditis elegans homologue of the yeast Erv29p, is essential for the endoplasmic reticulum (ER) export of the yolk protein VIT-2, which is synthesized as a lipoprotein complex. SFT-4 loss strongly inhibits the ER exit of yolk proteins and certain soluble cargo proteins in intestinal cells. SFT-4 predominantly localizes at ER exit sites (ERES) and physically interacts with VIT-2 in vivo, which suggests that SFT-4 promotes the ER export of soluble proteins as a cargo receptor. Notably, Surf4, a mammalian SFT-4 homologue, physically interacts with apolipoprotein B, a very-low-density lipoprotein core protein, and its loss causes ER accumulation of apolipoprotein B in human hepatic HepG2 cells. Interestingly, loss of SFT-4 and Surf4 reduced the number of COP II-positive ERES. Thus, SFT-4 and Surf4 regulate the export of soluble proteins, including lipoproteins, from the ER and participate in ERES organization in animals.
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