Abstract:
: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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Lee M,Fairn GDdoi
10.1016/j.bbrc.2018.01.138subject
Has Abstractpub_date
2018-02-19 00:00:00pages
1088-1094issue
4eissn
0006-291Xissn
1090-2104pii
S0006-291X(18)30159-1journal_volume
496pub_type
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journal_title:Biochemical and biophysical research communications
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更新日期:2019-01-22 00:00:00
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journal_title:Biochemical and biophysical research communications
pub_type: 杂志文章
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journal_title:Biochemical and biophysical research communications
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