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Ca^<2+> Release to Lumen from ADP-sensitive Phosphoenzyme E1PCa_2 without Bound K^+ of Sarcoplasmic Reticulum Ca^<2+>-ATPase
https://asahikawa-med.repo.nii.ac.jp/records/4042
https://asahikawa-med.repo.nii.ac.jp/records/40421200e256-8464-4798-9488-67874aa91bd1
名前 / ファイル | ライセンス | アクション |
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Item type | 学術雑誌論文 / Journal Article_02(1) | |||||
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公開日 | 2012-05-17 | |||||
タイトル | ||||||
タイトル | Ca^<2+> Release to Lumen from ADP-sensitive Phosphoenzyme E1PCa_2 without Bound K^+ of Sarcoplasmic Reticulum Ca^<2+>-ATPase | |||||
言語 | en | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者 |
山崎, 和生
× 山崎, 和生× Daiho, Takashi× Danko, Stefania× Suzuki, Hiroshi |
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書誌情報 |
Journal of Biological Chemistry 巻 285, 号 49, p. 38674-38683, 発行日 2010-12-01 |
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ISSN | ||||||
収録物識別子タイプ | PISSN | |||||
収録物識別子 | 0021-9258 | |||||
DOI | ||||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1074/jbc.M110.183343 | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | During Ca^<2+> transport by sarcoplasmic reticulum Ca^<2+>-ATPase, the conformation change of ADP-sensitive phosphoenzyme (E1PCa_2) to ADP-insensitive phosphoenzyme (E2PCa_2) is followed by rapid Ca^<2+> release into the lumen. Here, we find that in the absence of K^+, Ca^<2+> release occurs considerably faster than E1PCa_2 to E2PCa_2 conformation change. Therefore, the lumenal Ca^<2+> release pathway is open to some extent in the K^+-free E1PCa_2 structure. The Ca^<2+> affinity of this E1P is as high as that of the unphosphorylated ATPase (E1), indicating the Ca^<2+> binding sites are not disrupted. Thus, bound K^+ stabilizes the E1PCa_2 structure with occluded Ca^<2+>, keeping the Ca^<2+> pathway to the lumen closed. We found previously (Yamasaki, K., Wang, G., Daiho, T., Danko, S., and Suzuki, H. (2008) J. Biol. Chem. 283, 29144-29155) that the K^+ bound in E2P reduces the Ca^<2+> affinity essential for achieving the high physiological Ca^<2+> gradient and to fully open the lumenal Ca^<2+> gate for rapid Ca^<2+> release (E2PCa_2 → E2P + 2Ca^<2+>). These findings show that bound K^+ is critical for stabilizing both E1PCa_2 and E2P structures, thereby contributing to the structural changes that efficiently couple phosphoenzyme processing and Ca^<2+> handling. | |||||
言語 | en | |||||
注記 | ||||||
内容記述タイプ | Other | |||||
内容記述 | © 2010 by The American Society for Biochemistry and Molecular Biology, Inc. | |||||
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内容記述タイプ | Other | |||||
内容記述 | text | |||||
著者版フラグ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
フォーマット | ||||||
内容記述タイプ | Other | |||||
内容記述 | application/pdf | |||||
ID(XooNIps) | ||||||
値 | 20937807 | |||||
閲覧数(XooNIps) | ||||||
値 | 1135 | |||||
ダウンロード数(XooNIps) | ||||||
値 | 828 |