Dephosphorylation of perilipin by protein phosphatases present in rat adipocytes

FEBS Letters

Londos, Constantine¹  Vernon, Richard G³  Clifford, Gary M²  McCormick, Damion K.T²  Yeaman, Stephen J² 

[1] Laboratory of Cellular and Developmental Biology, NIDDK, National Institutes of Health, Bethesda, MD, USA;Department of Biochemistry and Genetics, The Medical School, University of Newcastle, Newcastle upon Tyne NE2 4HH, UK;Hannah Research Institute, Ayr, UK

关键词: Lipolysis;    Perilipin;    Protein phosphorylation;    Protein phosphatase;    Adipocyte;    HSL;    hormone sensitive lipase;    PKA;    cAMP-dependent protein kinase;    PP;    protein phosphatase;    OA;    okadaic acid;    I-2;    inhibitor 2;    SDS-PAGE;    sodium dodecyl sulphate polyacrylamide electrophoresis;   

DOI  :  10.1016/S0014-5793(98)01052-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

By incubating ³²P-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.

【 授权许可】

Unknown