期刊
NATURE COMMUNICATIONS
卷 8, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-017-00861-5
关键词
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资金
- Australian Research Council [DP130100457]
- National Health and Medical Research Council (NHMRC) of Australia [1041301]
- NHMRC Senior Research Fellowship
- Ministry of Science and Technology of the People's Republic of China [2016YFA0502004]
- NHMRC-ARC Dementia Research Development Fellowship
- National Health and Medical Research Council of Australia [APP1037320, APP1058565, APP569542]
- ARC Centre of Excellence in Convergent Bio-Nano Science and Technology
ORP5 and ORP8, members of the oxysterol-binding protein (OSBP)-related proteins (ORP) family, are endoplasmic reticulum membrane proteins implicated in lipid trafficking. ORP5 and ORP8 are reported to localize to endoplasmic reticulum-plasma membrane junctions via binding to phosphatidylinositol-4-phosphate (PtdIns(4)P), and act as a PtdIns(4)P/phosphatidylserine counter exchanger between the endoplasmic reticulum and plasma membrane. Here we provide evidence that the pleckstrin homology domain of ORP5/8 via PtdIns(4,5)P-2, and not PtdIns(4)P binding mediates the recruitment of ORP5/8 to endoplasmic reticulum-plasma membrane contact sites. The OSBP-related domain of ORP8 can extract and transport multiple phosphoinositides in vitro, and knocking down both ORP5 and ORP8 in cells increases the plasma membrane level of PtdIns(4,5)P-2 with little effect on PtdIns(4)P. Overall, our data show, for the first time, that phosphoinositides other than PtdIns (4)P can also serve as co-exchangers for the transport of cargo lipids by ORPs.
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