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ID 47057
本文ファイル
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著者
Ishida, Atsuhiko 大学院総合科学研究科 広大研究者総覧
Tsumura, Kumiko
Oue, Megu
Takenaka, Yasuhiro
Shigeri, Yasushi
Goshima, Naoki
Ishihara, Yasuhiro 大学院総合科学研究科 広大研究者総覧
Hirano, Tetsuo 大学院総合科学研究科 広大研究者総覧
Baba, Hiromi
Sueyoshi, Noriyuki
Kameshita, Isamu
Yamazaki, Takeshi 大学院総合科学研究科 広大研究者総覧
抄録(英)
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.
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.
掲載誌名
BioMed Research International
2013巻
開始ページ
134813
出版年月日
2013
出版者
Hindawi Publishing Corporation
ISSN
2314-6133
2314-6141
出版者DOI
PubMedID
言語
英語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
publisher
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.
関連情報URL
部局名
総合科学研究科