PC-TP/StARD2: Of membranes and metabolism

被引：40

作者：

Kang, Hye Won ^{[1
]}

Wei, Jie ^{[1
]}

Cohen, David E. ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Dept Med, Div Gastroenterol,Brigham & Womens Hosp, Boston, MA 02115 USA

来源：

TRENDS IN ENDOCRINOLOGY AND METABOLISM | 2010年 / 21卷 / 07期

关键词：

PHOSPHATIDYLCHOLINE TRANSFER PROTEIN; PHOSPHOLIPID-TRANSFER PROTEIN; PHOSPHATIDYLINOSITOL TRANSFER PROTEINS; TISSUE-SPECIFIC EXPRESSION; BROWN ADIPOSE-TISSUE; START DOMAIN; LIPOPROTEIN METABOLISM; LIPID METABOLOME; DEFICIENT MICE; GENE STRUCTURE;

D O I：

10.1016/j.tem.2010.02.001

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

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-a. 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.

引用

页码：449 / 456

页数：8

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