Identification and Characterization of CaMKP-N, Nuclear Calmodulin-Dependent Protein Kinase Phosphatase.
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- Takeuchi Masayuki
- Department of Biochemistry, Asahikatca Medical College
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- Ishida Atsuhiko
- Department of Biochemistry, Asahikatca Medical College
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- Kameshita Isamu
- Department of Biochemistry, Asahikatca Medical College Department of Life Sciences, Faculty of Agriculture, Kagawa University
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- Kitani Takako
- Department of Biochemistry, Asahikatca Medical College
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- Okuno Sachiko
- Department of Biochemistry, Asahikatca Medical College
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- Fujisawa Hitoshi
- Department of Biochemistry, Asahikatca Medical College
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Abstract
Calmodulin-dependent protein kinase phosphatase (CaMKP) dephosphorylates and concomitantly deactivates multifunctional Ca2+/calmodulin-dependent protein kinases (CaMKs), such as CaMKI, CaMKII, and CaMKIV. In the present study, a nuclear CaMKP-related protein, CaMKP-N, was identified. This protein consisted of 757 amino acid residues with a calculated molecular weight of 84, 176. Recombinant CaMKP-N dephosphorylated CaMKIV. The activity of CaMKP-N requires Mn2+ ions and is stimulated by polycations. Transiently expressed CaMKP-N in COS-7 cells was localized in the nucleus. This finding together with previous reports regarding localization of CaMKs indicates that CaMKP-N dephosphorylates CaMKIV and nuclear CaMKII, whereas CaMKP dephosphorylates CaMKI and cytosolic CaMKII.
Journal
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- The Journal of Biochemistry
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The Journal of Biochemistry 130 (6), 833-840, 2001
The Japanese Biochemical Society
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Details 詳細情報について
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- CRID
- 1390282679909053696
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- NII Article ID
- 130003534306
- 50001007588
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- NII Book ID
- AA00694073
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- COI
- 1:CAS:528:DC%2BD38XptFSjtA%3D%3D
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- ISSN
- 17562651
- 0021924X
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- NDL BIB ID
- 5997037
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- PubMed
- 11726284
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed