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Article

Phospholipase D activity is required for suppression of yeast phosphatidylinositol transfer protein defects.

Proceedings of the National Academy of Sciences of the United States of America - 13 Oct 1998

Xie Z, Fang M, Rivas M P, Faulkner A J, Sternweis P C, Engebrecht J A, Bankaitis V A

Abstract excerpt

Yeast phosphatidylinositol transfer protein (Sec14p) function is essential for production of Golgi-derived secretory vesicles, and this requirement is bypassed by mutations in at least seven genes. Analyses of such 'bypass Sec14p' mutants suggest that Sec14p acts to maintain an essential Golgi membrane diacylglycerol (DAG) pool that somehow acts to promote Golgi secretory function. SPO14 encodes the sole yeast...

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PMID: 9770489
DOI: 10.1073/pnas.95.21.12346
PMCID: PMC22834

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Phospholipase D activity is required for suppression of yeast phosphatidylinositol transfer protein defects.PMID 9770489Read ↗

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A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes.Semantic proximity Read ↗

Roles of phosphoinositides and of Spo14p (phospholipase D)-generated phosphatidic acid during yeast sporulation.Semantic proximity Read ↗

Identification of a novel, Ca(2+)-dependent phospholipase D with preference for phosphatidylserine and phosphatidylethanolamine in Saccharomyces cerevisiae.Semantic proximity Read ↗

Phospholipase D and the SNARE Sso1p are necessary for vesicle fusion during sporulation in yeast.Semantic proximity Read ↗

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