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Roles of Tyr122-hydrophobic cluster and K+ binding in Ca2+ -releasing process of ADP-insensitive phosphoenzyme of sarcoplasmic reticulum Ca2+ -ATPase
https://asahikawa-med.repo.nii.ac.jp/records/1341
https://asahikawa-med.repo.nii.ac.jp/records/1341db792286-41a5-4f5b-beb9-79a563ad765a
| 名前 / ファイル | ライセンス | アクション |
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1605.pdf (3.8 MB)
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| Item type | 学術雑誌論文 / Journal Article_02(1) | |||||||||||||||||
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| 公開日 | 2009-03-11 | |||||||||||||||||
| タイトル | ||||||||||||||||||
| タイトル | Roles of Tyr122-hydrophobic cluster and K+ binding in Ca2+ -releasing process of ADP-insensitive phosphoenzyme of sarcoplasmic reticulum Ca2+ -ATPase | |||||||||||||||||
| 言語 | en | |||||||||||||||||
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| 言語 | eng | |||||||||||||||||
| 資源タイプ | ||||||||||||||||||
| 資源タイプ | journal article | |||||||||||||||||
| 著者 |
山崎, 和生
× 山崎, 和生
× Wang, G
× Daiho, T
× Danko, S
× Suzuki, H
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| 著者 ローマ字 | ||||||||||||||||||
| Yamasaki, Kazuo | ||||||||||||||||||
| 書誌情報 |
Journal of Biological Chemistry 巻 283, 号 43, p. 29144-29155, 発行日 2008-10-01 |
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| 収録物識別子タイプ | ISSN | |||||||||||||||||
| 収録物識別子 | 0021-9258 | |||||||||||||||||
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| 関連タイプ | isVersionOf | |||||||||||||||||
| 識別子タイプ | DOI | |||||||||||||||||
| 関連識別子 | 10.1074/jbc.M804596200 | |||||||||||||||||
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| 内容記述タイプ | Other | |||||||||||||||||
| 内容記述 | http://www.ncbi.nlm.nih.gov/pubmed/18728008 | http://www.ncbi.nlm.nih.gov/pubmed/18728008 | |||||||||||||||||
| 抄録 | ||||||||||||||||||
| 内容記述タイプ | Abstract | |||||||||||||||||
| 内容記述 | Tyr(122)-hydrophobic cluster (Y122-HC) is an interaction network formed by the top part of the second transmembrane helix and the cytoplasmic actuator and phosphorylation domains of sarcoplasmic reticulum Ca(2+)-ATPase. We have previously found that Y122-HC plays critical roles in the processing of ADP-insensitive phosphoenzyme (E2P) after its formation by the isomerization from ADP-sensitive phosphoenzyme (E1PCa(2)) (Wang, G., Yamasaki, K., Daiho, T., and Suzuki, H. (2005) J. Biol. Chem. 280, 26508-26516). Here, we further explored kinetic properties of the alanine-substitution mutants of Y122-HC to examine roles of Y122-HC for Ca(2+) release process in E2P. In the steady state, the amount of E2P decreased so that of E1PCa(2) increased with increasing lumenal Ca(2+) concentration in the mutants with K(0.5) 110-320 microm at pH 7.3. These lumenal Ca(2+) affinities in E2P agreed with those estimated from the forward and lumenal Ca(2+)-induced reverse kinetics of the E1PCa(2)-E2P isomerization. K(0.5) of the wild type in the kinetics was estimated to be 1.5 mM. Thus, E2P of the mutants possesses significantly higher affinities for lumenal Ca(2+) than that of the wild type. The kinetics further indicated that the rates of lumenal Ca(2+) access and binding to the transport sites of E2P were substantially slowed by the mutations. Therefore, the proper formation of Y122-HC and resulting compactly organized structure are critical for both decreasing Ca(2+) affinity and opening the lumenal gate, thus for Ca(2+) release from E2PCa(2). Interestingly, when K(+) was omitted from the medium of the wild type, the properties of the wild type became similar to those of Y122-HC mutants. K(+) binding likely functions via producing the compactly organized structure, in this sense, similarly to Y122-HC. | |||||||||||||||||
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| 内容記述タイプ | Other | |||||||||||||||||
| 注記 | author | |||||||||||||||||
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| 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) | ||||||||||||||||||
| 18728008 | ||||||||||||||||||
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| ダウンロード数(XooNIps) | ||||||||||||||||||
| 1255 | ||||||||||||||||||
