| Literature DB >> 20338778 |
Hye Won Kang1, Jie Wei, David E Cohen.
Abstract
Phosphatidylcholine transfer protein (PC-TP, synonym StARD2) binds phosphatidylcholines, and catalyzes their intermembrane transfer and exchange in vitro. The structure of PC-TP comprises a hydrophobic pocket and a well-defined head group binding site, and its gene expression is regulated by peroxisome proliferator activated receptor-alpha. Recent studies have revealed key regulatory roles for PC-TP in lipid and glucose metabolism. Notably, Pctp(-/-) mice are sensitized to the action of insulin, and exhibit more efficient brown fat-mediated thermogenesis. PC-TP appears to limit access of fatty acids to mitochondria by stimulating the activity of thioesterase superfamily member 2, a newly characterized long-chain fatty acyl-coenzyme A thioesterase. Because PC-TP discriminates between phosphatidylcholines within lipid bilayers, it might function as a sensor that links metabolic regulation to membrane composition. Copyright 2010 Elsevier Ltd. All rights reserved.Entities:
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Year: 2010 PMID: 20338778 PMCID: PMC2897958 DOI: 10.1016/j.tem.2010.02.001
Source DB: PubMed Journal: Trends Endocrinol Metab ISSN: 1043-2760 Impact factor: 12.015