| 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 |
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|
タイトル |
An Active C-Terminally Truncated Form of Ca2+/Calmodulin-Dependent Protein Kinase Phosphatase-N (CaMKP-N/PPM1E) |
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言語 |
en |
| 作成者 |
Ishida, Atsuhiko
Tsumura, Kumiko
Oue, Megu
Takenaka, Yasuhiro
Shigeri, Yasushi
Goshima, Naoki
Ishihara, Yasuhiro
Hirano, Tetsuo
Baba, Hiromi
Sueyoshi, Noriyuki
Kameshita, Isamu
Yamazaki, Takeshi
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| アクセス権 |
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アクセス権 |
open access |
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アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 権利情報 |
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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 |
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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. |
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言語 |
en |
| 内容記述 |
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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 |
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出版者 |
Hindawi Publishing Corporation |
| 言語 |
|
|
言語 |
eng |
| 資源タイプ |
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|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| 出版タイプ |
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出版タイプ |
VoR |
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出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| 関連情報 |
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|
識別子タイプ |
DOI |
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|
関連識別子 |
http://dx.doi.org/10.1155/2013/134813 |
| 関連情報 |
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|
識別子タイプ |
DOI |
|
|
関連識別子 |
10.1155/2013/134813 |
| 関連情報 |
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|
識別子タイプ |
PMID |
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関連識別子 |
23991411 |
| 収録物識別子 |
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収録物識別子タイプ |
ISSN |
|
収録物識別子 |
2314-6133 |
| 収録物識別子 |
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|
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 |
134813.pdf (1.7 MB)
