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Phosphorylation of calmodulin by Ca2+/calmodulin-dependent protein kinase IV
https://asahikawa-med.repo.nii.ac.jp/records/577
https://asahikawa-med.repo.nii.ac.jp/records/577fde5b72a-dd4e-4c35-9115-49645b004a56
| 名前 / ファイル | ライセンス | アクション |
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716.pdf (406.8 kB)
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| Item type | 学術雑誌論文 / Journal Article_02(1) | |||||||||||||||||
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| 公開日 | 2007-08-24 | |||||||||||||||||
| タイトル | ||||||||||||||||||
| タイトル | Phosphorylation of calmodulin by Ca2+/calmodulin-dependent protein kinase IV | |||||||||||||||||
| 言語 | en | |||||||||||||||||
| 言語 | ||||||||||||||||||
| 言語 | eng | |||||||||||||||||
| 資源タイプ | ||||||||||||||||||
| 資源タイプ | journal article | |||||||||||||||||
| 著者 |
石田, 敦彦
× 石田, 敦彦
× Kameshita, I
× Okuno, S
× Kitani, T
× Fujisawa, H
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| 著者 ローマ字 | ||||||||||||||||||
| 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 | ||||||||||||||||||
| 収録物識別子タイプ | ISSN | |||||||||||||||||
| 収録物識別子 | 0003-9861 | |||||||||||||||||
| DOI | ||||||||||||||||||
| 関連タイプ | isVersionOf | |||||||||||||||||
| 識別子タイプ | DOI | |||||||||||||||||
| 関連識別子 | 10.1016/S0003-9861(02)00514-3 | |||||||||||||||||
| リンクURL | ||||||||||||||||||
| 内容記述タイプ | Other | |||||||||||||||||
| 内容記述 | http://www.science-direct.com/science/journal/00039861 | http://www.science-direct.com/science/journal/00039861 | |||||||||||||||||
| 抄録 | ||||||||||||||||||
| 内容記述タイプ | Abstract | |||||||||||||||||
| 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 | ||||||||||||||||||
| 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 |
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| 資源タイプ | ||||||||||||||||||
| 内容記述タイプ | Other | |||||||||||||||||
| 資源タイプ | text | |||||||||||||||||
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| 出版タイプ | AM | |||||||||||||||||
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| 内容記述タイプ | Other | |||||||||||||||||
| 内容記述 | application/pdf | |||||||||||||||||
| ID(XooNIps) | ||||||||||||||||||
| 12392717 | ||||||||||||||||||
| 閲覧数(XooNIps) | ||||||||||||||||||
| ダウンロード数(XooNIps) | ||||||||||||||||||
| 1667 | ||||||||||||||||||
