Dephosphorylation of perilipin by protein phosphatases present in rat adipocytes

被引：31

作者：

Clifford, GM

McCormick, DKT

Londos, C

Vernon, RG

Yeaman, SJ ^{[1
]}

机构：

[1] Univ Newcastle, Sch Med, Dept Biochem & Genet, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England

[2] NIDDK, Cellular & Dev Biol Lab, NIH, Bethesda, MD USA

[3] Hannah Res Inst, Ayr KA6 5HL, Scotland

来源：

FEBS LETTERS | 1998年 / 435卷 / 01期

基金：

英国生物技术与生命科学研究理事会;

关键词：

lipolysis; perilipin; protein phosphorylation; protein phosphatase; adipocyte;

D O I：

10.1016/S0014-5793(98)01052-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

By incubating P-32-labelled adipocytes, and extracts from these cells, in the presence or absence of specific inhibitors, we evaluated the contribution of protein phosphatases PP1, PP2A and PP2C, to the dephosphorylation of perilipin, an acutely hormone-regulated adipocyte phosphoprotein. Under conditions to completely inhibit PP2A activity, perilipin phosphatase activity in extracts remain unaffected, but PP1 inhibition results in abolition of perilipin phosphatase activity. Inhibition of PP1 (and 2A) in intact adipocytes stimulated lipolysis and increased phosphorylation of perilipin. No involvement of PP2C was found. Hence, PP1 constitutes the predominant if not sole perilipin phosphatase in adipocytes. (C) 1998 Federation of European Biochemical Societies.

引用

页码：125 / 129

页数：5

共 29 条

[1] Identification of novel phosphorylation sites in hormone-sensitive lipase that are phosphorylated in response to isoproterenol and govern activation properties in vitro [J].