Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 496, Issue 4, Pages 1088-1094Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2018.01.138
Keywords
ER-PM contacts; Phospholipids; Oxysterol-binding protein-related proteins (ORP)
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Funding
- Canadian Institutes of Health Research (CIHR)
- Government of Ontario
- Li Ka Shing Knowledge Institute
- Government of Ontario Graduate Scholarship
- [MOP-133656]
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Oxysterol-binding protein-related proteins are implicated in the sensing and transporting lipids at the membrane contact sites. One of the members of the mammalian ORP family, ORP8, is thought to transport lipids through directly tethering both ER and PM membranes. Targeting to PM is thought to be mediated by N-terminal pleckstrin homology domain via binding to phosphoinositides. Sequence alignments and NMR structural determination revealed that the PH domain of ORP8 is atypical and contains an insertion of 20 amino acids in an unstructured loop region that may potentially block interactions with ligands. Using standard lipid-protein overlay assays or liposomal binding assays we could not detect binding of a recombinant version of the PH domain. Examination of a series of deletion constructs demonstrated that both the N-terminal polybasic region and the PH domain are required for proper targeting of the short splice variant ORP8S to the PM-ER contact site in Chinese hamster ovary cells. Crown Copyright (C) 2018 Published by Elsevier Inc. All rights reserved.
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