Matches in SemOpenAlex for { <https://semopenalex.org/work/W1010587218> ?p ?o ?g. }
Showing items 1 to 57 of
57
with 100 items per page.
- W1010587218 abstract "Phosphatidylserine (PS) synthase catalyzes the committed step of phosphatidylcholine synthesis via the CDP-diacylglycerol pathway in the yeast Saccharomyces cerevisiae. It is one of the most highly regulated phospholipid synthesis enzymes in yeast. Previous work showed that PS synthase is phosphorylated by protein kinase A, and that phosphorylation inhibited enzyme activity. In this work, the sites of protein kinase A phosphorylation were examined. Upon SDS-PAGE, the PS synthase migrates as a doublet of two protein bands. Protein kinase A phosphorylation of the native enzyme resulted in the disappearance of the lower protein band, whereas treatment with alkaline phosphatase or protein phosphatase resulted in the disappearance of the upper protein band. A site-directed mutagenesis analysis of putative protein kinase A sites (Ser46, Ser47, Ser140, Ser141) revealed that Ser46 and Ser47 were the major phosphorylation sites in the enzyme. A double S46A S47A mutation resulted in an enzyme that migrated on SDS-gels as a single protein band, whereas single S46A and S47A mutant proteins migrated as doublets with a decrease in the abundance of the upper band. PS synthase was also subject to proteolytic degradation, and the phosphorylation of the enzyme at Ser46 and Ser47 protected the enzyme from proteolysis. Supported by NIH grant GM 50679." @default.
- W1010587218 created "2016-06-24" @default.
- W1010587218 creator A5015880535 @default.
- W1010587218 creator A5089452267 @default.
- W1010587218 date "2009-04-01" @default.
- W1010587218 modified "2023-10-16" @default.
- W1010587218 title "Phosphorylation of Yeast Phosphatidylserine Synthase by Protein Kinase A" @default.
- W1010587218 doi "https://doi.org/10.1096/fasebj.23.1_supplement.689.3" @default.
- W1010587218 hasPublicationYear "2009" @default.
- W1010587218 type Work @default.
- W1010587218 sameAs 1010587218 @default.
- W1010587218 citedByCount "0" @default.
- W1010587218 crossrefType "journal-article" @default.
- W1010587218 hasAuthorship W1010587218A5015880535 @default.
- W1010587218 hasAuthorship W1010587218A5089452267 @default.
- W1010587218 hasConcept C11960822 @default.
- W1010587218 hasConcept C184235292 @default.
- W1010587218 hasConcept C185592680 @default.
- W1010587218 hasConcept C2778918659 @default.
- W1010587218 hasConcept C2779222958 @default.
- W1010587218 hasConcept C2779637612 @default.
- W1010587218 hasConcept C41625074 @default.
- W1010587218 hasConcept C55493867 @default.
- W1010587218 hasConcept C86803240 @default.
- W1010587218 hasConcept C95444343 @default.
- W1010587218 hasConcept C97029542 @default.
- W1010587218 hasConceptScore W1010587218C11960822 @default.
- W1010587218 hasConceptScore W1010587218C184235292 @default.
- W1010587218 hasConceptScore W1010587218C185592680 @default.
- W1010587218 hasConceptScore W1010587218C2778918659 @default.
- W1010587218 hasConceptScore W1010587218C2779222958 @default.
- W1010587218 hasConceptScore W1010587218C2779637612 @default.
- W1010587218 hasConceptScore W1010587218C41625074 @default.
- W1010587218 hasConceptScore W1010587218C55493867 @default.
- W1010587218 hasConceptScore W1010587218C86803240 @default.
- W1010587218 hasConceptScore W1010587218C95444343 @default.
- W1010587218 hasConceptScore W1010587218C97029542 @default.
- W1010587218 hasFunder F4320332161 @default.
- W1010587218 hasIssue "S1" @default.
- W1010587218 hasLocation W10105872181 @default.
- W1010587218 hasOpenAccess W1010587218 @default.
- W1010587218 hasPrimaryLocation W10105872181 @default.
- W1010587218 hasRelatedWork W1520436089 @default.
- W1010587218 hasRelatedWork W2023965833 @default.
- W1010587218 hasRelatedWork W2047183378 @default.
- W1010587218 hasRelatedWork W2052131670 @default.
- W1010587218 hasRelatedWork W2058545848 @default.
- W1010587218 hasRelatedWork W2066589921 @default.
- W1010587218 hasRelatedWork W2403122645 @default.
- W1010587218 hasRelatedWork W2410686946 @default.
- W1010587218 hasRelatedWork W2916357899 @default.
- W1010587218 hasRelatedWork W2136545008 @default.
- W1010587218 hasVolume "23" @default.
- W1010587218 isParatext "false" @default.
- W1010587218 isRetracted "false" @default.
- W1010587218 magId "1010587218" @default.
- W1010587218 workType "article" @default.