Identification of a 42 kDa protein as a substrate of protein phosphatase 1 in cilia from Paramecium

FEBS Letters

Schultz, Joachim E.¹  Klumpp, Susanne¹ 

[1]Pharmazeutisches Itistitut der Universität, Morgenstelle 8, D-7400 Tübingen, Germany

关键词: Protein phosphatase;    Paramecium;    Okadaic acid;    cAMP;    Ca-channel;    Cilia;   

DOI  :  10.1016/0014-5793(91)81003-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Okadaic acid, a specific inhibitor of protein phosphatase 1 in Paramecium causes sustained backward swimming in response to depolarising stimuli (S. Klumpp et al. (1990) EMBO J. 9, 685). Here, we employ okadaic acid, tautomycin, microcystin LR and inhibitor 1 as phosphatase inhibitors to identify a 42 kDa protein in the excitable ciliary membrane that is dephosphorylated by protein phosphatase 1. Identification of the 42 kDa protein was facilitated by the finding that the protein kinase responsible for its phosphorylation uses Ca-ATP as a substrate just as effectively as Mg-ATP. Notably, dephosphorylation of the 42 kDa protein is specifically inhibited by cyclic AMP; cyclic GMP has no effect.

【 授权许可】

Unknown