| 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 |
Phosphorylation of calmodulin by Ca2+/calmodulin-dependent protein kinase IV |
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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
Kameshita, I
Okuno, S
Kitani, T
Fujisawa, H
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| 著者 ローマ字 |
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Ishida, Atsuhiko |
| 書誌情報 |
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
巻 407,
号 1,
p. 72-82,
発行日 2002-11-01
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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/S0003-9861(02)00514-3 |
| 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 |
Calmodulin-dependent protein kinase IV (CaM-kinase IV) phosphorylated calmodulin (CaM), which is its own activator, in a poly--Lys [poly(Lys)]-dependent manner. Although CaM-kinase II weakly phosphorylated CaM under the same conditions, CaM-kinase I, CaM-kinase kinase α, and cAMP-dependent protein kinase did not phosphorylate CaM. Polycations such as poly(Lys) were required for the phosphorylation. The optimum concentration of poly(Lys) for the phosphorylation of 1 μM CaM was about 10 μg/ml, but poly(Lys) strongly inhibited CaM-kinase IV activity toward syntide-2 at this concentration, suggesting that the phosphorylation of CaM is not due to simple activation of the catalytic activity. Poly--Arg could partially substitute for poly(Lys), but protamine, spermine, and poly--Glu/Lys/Tyr (6/3/1) could not. When phosphorylation was carried out in the presence of poly(Lys) having various molecular weights, poly(Lys) with a higher molecular weight resulted in a higher degree of phosphorylation. Binding experiments using fluorescence polarization suggested that poly(Lys) mediates interaction between the CaM-kinase IV/CaM complex and another CaM. The ^<32>P-labeled CaM was digested with BrCN and Achromobacter protease I, and the resulting peptides were purified by reversed-phase HPLC. Automated Edman sequence analysis of the peptides, together with phosphoamino acid analysis, indicated that the major phosphorylation site was Thr^<44>. Activation of CaM-kinase II by the phosphorylated CaM was significantly lower than that by the nonphosphorylated CaM. Thus, CaM-kinase IV activated by binding Ca^<2+>/CaM can bind and phosphorylate another CaM with the aid of poly(Lys), leading to a decrease in the activity of CaM. |
| 注記 |
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内容記述タイプ |
Other |
|
注記 |
Elsevier, Ishida, A. ; Kameshita, I. ; Okuno, S. ; Kitani, T. ; Fujisawa, H., ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 407(1), 2002, 72-82
\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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12392717 |
| 閲覧数(XooNIps) |
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| ダウンロード数(XooNIps) |
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1667 |
716.pdf (406.8 kB)
