Dephosphorylation of PKCδ by protein phosphatase 2Ac and its inhibition by nucleotides

FEBS Letters

Goris, Jozef³  Parker, Peter J²  Dilworth, Stephen M¹  Srivastava, Jyoti² 

[1] Department of Metabolic Medicine, Imperial College School of Medicine, Hammersmith Hospital, Du Cane Road, London W12 0NN, UK;Protein Phosphorylation Laboratory, Cancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, UK;Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit Leuven, Herestraat 49, B-3000 Leuven, Belgium

关键词: Protein kinase Cδ;    Protein phosphatase;    PP1;    PP2C;    PP2A;    Dephosphorylation;   

DOI  :  10.1016/S0014-5793(02)02500-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The protein phosphatases PP1_c, PP2A_c and PP2Cα are shown to dephosphorylate protein kinase Cδ (PKCδ) in vitro; of these PP2A_c displayed the highest specific activity towards PKCδ. The role of PP2A_c in the dephosphorylation of PKCδ in cells was supported by the demonstration that these proteins could be co-immunoprecipitated from NIH3T3 cells. However the observation that binding of Mg-ATP to PKCδ could protect the enzyme from dephosphorylation by PP2A_c in vitro indicates that an additional input/factor is required for dephosphorylation in vivo.

【 授权许可】

Unknown