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An Active C-Terminally Truncated Form of Ca2+/Calmodulin-Dependent Protein Kinase Phosphatase-N (CaMKP-N/PPM1E)

https://hiroshima.repo.nii.ac.jp/records/2006456
https://hiroshima.repo.nii.ac.jp/records/2006456
350348dd-2bbd-46a4-b4db-cd88b295dc8a
名前 / ファイル ライセンス アクション
134813.pdf 134813.pdf (1.7 MB)
Item type デフォルトアイテムタイプ_(フル)(1)
公開日 2023-03-18
タイトル
タイトル An Active C-Terminally Truncated Form of Ca2+/Calmodulin-Dependent Protein Kinase Phosphatase-N (CaMKP-N/PPM1E)
言語 en
作成者 Ishida, Atsuhiko

× Ishida, Atsuhiko

en Ishida, Atsuhiko

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Tsumura, Kumiko

× Tsumura, Kumiko

en Tsumura, Kumiko

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Oue, Megu

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en Oue, Megu

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Takenaka, Yasuhiro

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Shigeri, Yasushi

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en Shigeri, Yasushi

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Goshima, Naoki

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en Goshima, Naoki

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Ishihara, Yasuhiro

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Hirano, Tetsuo

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Baba, Hiromi

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Sueyoshi, Noriyuki

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Kameshita, Isamu

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Yamazaki, Takeshi

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en Yamazaki, Takeshi

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アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利情報
権利情報 Copyright © 2013 Atsuhiko Ishida et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
内容記述
内容記述 Ca2+/calmodulin-dependent protein kinase phosphatase (CaMKP/PPM1F) and its nuclear homolog CaMKP-N (PPM1E) are Ser/Thr protein phosphatases that belong to the PPM family. CaMKP-N is expressed in the brain and undergoes proteolytic processing to yield a C-terminally truncated form. The physiological significance of this processing, however, is not fully understood. Using a wheat-embryo cell-free protein expression system, we prepared human CaMKP-N (hCaMKP-N(WT)) and the truncated form, hCaMKP-N(1–559), to compare their enzymatic properties using a phosphopeptide substrate. The hCaMKP-N(1–559) exhibited a much higher value than the hCaMKP-N(WT) did, suggesting that the processing may be a regulatory mechanism to generate a more active species. The active form, hCaMKP-N(1–559), showed Mn2+ or Mg2+-dependent phosphatase activity with a strong preference for phospho-Thr residues and was severely inhibited by NaF, but not by okadaic acid, calyculin A, or 1-amino-8-naphthol-2,4-disulfonic acid, a specific inhibitor of CaMKP. It could bind to postsynaptic density and dephosphorylate the autophosphorylated Ca2+/calmodulin-dependent protein kinase II. Furthermore, it was inactivated by H2O2 treatment, and the inactivation was completely reversed by treatment with DTT, implying that this process is reversibly regulated by oxidation/reduction. The truncated CaMKP-N may play an important physiological role in neuronal cells.
言語 en
内容記述
内容記述タイプ Other
内容記述 This work was supported, in part, by Grants-in-Aid for Scientific Research (21590334) from the Ministry of Education, Science, Sports, and Culture of Japan and by a grant from the Japan Foundation for Applied Enzymology.
出版者
出版者 Hindawi Publishing Corporation
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
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連情報
識別子タイプ DOI
関連識別子 http://dx.doi.org/10.1155/2013/134813
関連情報
識別子タイプ DOI
関連識別子 10.1155/2013/134813
関連情報
識別子タイプ PMID
関連識別子 23991411
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 2314-6133
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 2314-6141
開始ページ
開始ページ 134813
書誌情報 BioMed Research International
BioMed Research International

巻 2013, p. 134813, 発行日 2013
旧ID 47057
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