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Identification of a 42 kDa protein as a substrate of protein phosphatase 1 in cilia from Paramecium.
- Source :
-
FEBS letters [FEBS Lett] 1991 Aug 19; Vol. 288 (1-2), pp. 60-4. - Publication Year :
- 1991
-
Abstract
- 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.
- Subjects :
- Animals
Antifungal Agents pharmacology
Calcium Channels metabolism
Calcium-Transporting ATPases metabolism
Cilia enzymology
Cyclic AMP metabolism
Ethers, Cyclic pharmacology
Marine Toxins
Microcystins
Okadaic Acid
Paramecium drug effects
Peptides, Cyclic pharmacology
Phosphoprotein Phosphatases drug effects
Phosphoproteins metabolism
Phosphorylation drug effects
Protein Phosphatase 1
Protozoan Proteins metabolism
Cilia chemistry
Paramecium analysis
Phosphoprotein Phosphatases metabolism
Phosphoproteins isolation & purification
Protozoan Proteins isolation & purification
Pyrans
Spiro Compounds
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 288
- Issue :
- 1-2
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 1652480
- Full Text :
- https://doi.org/10.1016/0014-5793(91)81003-q