Dephosphorylation of perilipin by protein phosphatases present in rat adipocytes.
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.
Department of Biochemistry and Genetics, The Medical School, University of Newcastle, Newcastle upon Tyne, UK.
G M
GM
Clifford
D K
DK
McCormick
C
C
Londos
R G
RG
Vernon
S J
SJ
Yeaman
D017667:Adipocytes / Q000187:drug effects / Q000201:enzymology* / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins; D008066:Lipolysis / Q000187:drug effects; D008297:Male; D019319:Okadaic Acid / Q000494:pharmacology; D000070778:Perilipin-1; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D010750:Phosphoproteins / Q000187:drug effects / Q000378:metabolism*; D010766:Phosphorylation; D051381:Rats; D017208:Rats, Wistar
D002352:Carrier Proteins; D000070778:Perilipin-1; D010750:Phosphoproteins; D019319:Okadaic Acid; D010749:Phosphoprotein Phosphatases