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Acute effects of insulin on the activity of mitochondrial GPAT1 in primary adipocytes.

Authors: Bronnikov, GE  Aboulaich, N  Vener, AV  Stralfors, P 
Citation: Bronnikov GE, etal., Biochem Biophys Res Commun. 2008 Feb 29;367(1):201-7. Epub 2007 Dec 31.
Pubmed: (View Article at PubMed) PMID:18167308
DOI: Full-text: DOI:10.1016/j.bbrc.2007.12.127

The mitochondrial enzyme 1-acyl-sn-glycerol-3-phosphate acyltransferase (mtGPAT1) catalyzes a rate-limiting step in triacylglycerol and glycerophospholipid biosynthesis, which can be modulated by protein kinases in cell free analyses. We report that treatment of primary rat adipocytes with insulin acutely affects the activity of mtGPAT1 by increasing V(MAX) and K(M) for the substrates glycerol-3-phosphate and palmitoyl-CoA. Proteolytic cleavage of isolated mitochondrial membranes and mass spectrometric peptide sequencing identify in vivo phosphorylation of serine 632 and serine 639 in mtGPAT1. These phosphorylation sites correspond to casein kinase-2 consensus sequences and are highly conserved in chordate animal, but not fly, fungal or plant, mtGPAT1.

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CRRD Object Information
CRRD ID: 2313661
Created: 2009-10-07
Species: All species
Last Modified: 2009-10-07
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.