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Identification of a 42 kDa protein as a substrate of protein phosphatase 1 in cilia from Paramecium
Author(s) -
Klumpp Susanne,
Schultz Joachim E.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81003-q
Subject(s) - okadaic acid , dephosphorylation , phosphatase , paramecium , phosphorylation , biochemistry , protein kinase a , protein phosphorylation , protein phosphatase 1 , protein phosphatase 2 , biology , chemistry , microbiology and biotechnology
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.