-
Views
-
Cite
Cite
Takako Kitani, Atsuhiko Ishida, Sachiko Okuno, Masayuki Takeuchi, Isamu Kameshita, Hitoshi Fujisawa, Molecular Cloning of Ca2+/Calmodulin-Dependent Protein Kinase Phosphatase, The Journal of Biochemistry, Volume 125, Issue 6, June 1999, Pages 1022–1028, https://doi.org/10.1093/oxfordjournals.jbchem.a022381
- Share Icon Share
Abstract
Calmodulin-dependent protein kinase (CaM-kinase) phosphatase dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase [Ishida,I., Okuno,S., Kitani,T., Kameshita, I., and Fujisawa, H. (1998) Biochem. Biophys. Res. Commun. 253, 159–163], suggesting that CaM-kinase phosphatase plays important roles in the function of Ca2+ in the cell, because the three multifunctional CaM-kinases (CaM-kinases I, II, and IV) are thought to be the key enzymes in the Ca2+-signaling system. In the present study, cDNA for CaM-kinase phosphatase was cloned from a rat brain cDNA library. The coded protein consisted of 450 amino acids with a molecular weight of 49,165. Western blot analysis showed the ubiquitous tissue distribution of CaM-kinase phosphatase. Immunocytochemical analysis revealed that CaM-kinase phosphatase is evenly distributed outside the nucleus in a cell.