Title : Lipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues.

Pub. Date : 2009 Dec 14

PMID : 20008566






3 Functional Relationships(s)
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Protein Name
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1 Using Osh4p/Kes1p as a representative ORP, we show that ORPs have at least two membrane-binding surfaces; one near the mouth of the sterol-binding pocket and a distal site that can bind a second membrane. Sterols oxysterol-binding protein KES1 Saccharomyces cerevisiae S288C
2 Using Osh4p/Kes1p as a representative ORP, we show that ORPs have at least two membrane-binding surfaces; one near the mouth of the sterol-binding pocket and a distal site that can bind a second membrane. Sterols oxysterol-binding protein KES1 Saccharomyces cerevisiae S288C
3 The distal site is required for the protein to function in cells and, remarkably, regulates the rate at which Osh4p extracts and delivers sterols in a phosphoinositide-dependent manner. Sterols oxysterol-binding protein KES1 Saccharomyces cerevisiae S288C