ORP5 and ORP8 bind phosphatidylinositol-4, 5-biphosphate (PtdIns(4,5)P 2) and regulate its level at the plasma membrane

Rajesh Ghai, Ximing Du, Huan Wang, Jiangqing Dong, Charles Ferguson, Andrew J. Brown, Robert G. Parton, Jia-Wei Wu () and Hongyuan Yang ()
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Rajesh Ghai: The University of New South Wales
Ximing Du: The University of New South Wales
Huan Wang: Tsinghua University
Jiangqing Dong: Tsinghua University
Charles Ferguson: The University of Queensland
Andrew J. Brown: The University of New South Wales
Robert G. Parton: The University of Queensland
Jia-Wei Wu: Tsinghua University
Hongyuan Yang: The University of New South Wales

Nature Communications, 2017, vol. 8, issue 1, 1-14

Abstract: Abstract 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.

Date: 2017
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DOI: 10.1038/s41467-017-00861-5

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