Proteomic analysis of yeast membranes enriched in acyltransferases Gpt2p and Sct1p provides insight into their roles and regulation

Date
2017
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Abstract
Gpt2p and Sct1p are yeast glycerol-3-phosphate acyltransferases (GPATs) that catalyze the first committed and rate-limiting step in the synthesis of glycerolipids. Although both enzymes catalyze the same reaction, they contribute differentially to downstream steps in the de novo biosynthesis of glycerolipids. Membranes enriched in either Gpt2p or Sct1p were affinity isolated and associated proteins were identified by mass spectrometry. Unique protein profiles were identified for both GPATs, with significant enrichments in proteins related to glycerophospholipid, sphingolipid, and fatty acid metabolism. Identified proteins revealed a hub around palmitoyl-CoA, implying that there is competition between these pathways for the channelling of this fatty acid into specific metabolic branches. Interestingly, a Gpt2p mutant missing its serine-rich C-terminus did not associate with selected proteins found in the wildtype Gpt2p-enriched membranes. This suggests that this protein region of high phosphorylation in Gpt2p may be important in facilitating some protein-protein associations detected in this study.
Description
Keywords
Biology, Biochemistry
Citation
Shabits, B. (2017). Proteomic analysis of yeast membranes enriched in acyltransferases Gpt2p and Sct1p provides insight into their roles and regulation (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/27471