| Item type |
学術雑誌論文 / Journal Article_02(1) |
| 公開日 |
2007-08-24 |
| タイトル |
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タイトル |
Identification of major Ca^<2+>/calmodulin-dependent protein kinase phosphatase-binding proteins in brain. Biochemical analysis of the interaction. |
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言語 |
en |
| 言語 |
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言語 |
eng |
| 資源タイプ |
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資源タイプ |
journal article |
| 著者 |
石田, 敦彦
Tada, Y
Nimura, T
Sueyoshi, N
Kato, T
Takeuchi, M
Fujisawa, H
Taniguchi, T
Kameshita, I
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| 著者 ローマ字 |
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|
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Ishida, Atsuhiko |
| 書誌情報 |
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
巻 435,
号 1,
p. 134-146,
発行日 2005-03-01
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| ISSN |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
0003-9861 |
| DOI |
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関連タイプ |
isVersionOf |
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識別子タイプ |
DOI |
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関連識別子 |
10.1016/j.abb.2004.11.022 |
| リンクURL |
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内容記述タイプ |
Other |
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内容記述 |
http://www.science-direct.com/science/journal/00039861 | http://www.science-direct.com/science/journal/00039861 |
| 抄録 |
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内容記述タイプ |
Abstract |
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内容記述 |
Ca^<2+>/calmodulin-dependent protein kinase phosphatase (CaMKP) is a unique protein phosphatase that specifically dephosphorylates and regulates multifunctional Ca^<2+>/calmodulin-dependent protein kinases (CaMKs). To clarify the physiological significance of CaMKP, we identified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and fructose bisphosphate aldolase as major binding partners of CaMKP in a soluble fraction of rat brain using the two-dimensional far-Western blotting technique, in conjunction with peptide mass fingerprinting analysis. We analyzed the affinities of these interactions. Wild type CaMKP–glutathione S-transferase (GST) associated with GAPDH in a GST pull-down assay. Deletion analysis suggested that the N-terminal side of the catalytic domain of CaMKP was responsible for the binding to GAPDH. Further, anti-CaMKP antibody coimmunoprecipitated GAPDH in a rat brain extract. GAPDH was phosphorylated by CaMKI or CaMKIV in vitro; however, when CaMKP coexisted, the phosphorylation was markedly attenuated. Under these conditions, CaMKP significantly dephosphorylated CaMKI and CaMKIV, which had been phosphorylated by CaMK kinase, whereas it did not dephosphorylate the previously phosphorylated GAPDH. The results suggest that CaMKP regulates the phosphorylation level of GAPDH in the CaMKP–GAPDH complex by dephosphorylating and deactivating CaMKs that are responsible for the phosphorylation of GAPDH. |
| 注記 |
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内容記述タイプ |
Other |
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注記 |
Elsevier, Ishida, A. ; Tada, Y. ; Nimura, T. ; Sueyoshi, N. ; Katoh, T. ; Takeuchi, M. ; Fujisawa, H. ; Taniguchi, T. ; Kameshita, I., ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 435(1), 2005, 134-146.
\nauthor |
| 資源タイプ |
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内容記述タイプ |
Other |
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資源タイプ |
text |
| 著者版フラグ |
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出版タイプ |
AM |
| フォーマット |
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内容記述タイプ |
Other |
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内容記述 |
application/pdf |
| ID(XooNIps) |
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15680915 |
| 閲覧数(XooNIps) |
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| ダウンロード数(XooNIps) |
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1452 |
710.pdf (370.0 kB)
