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Tyrosine phosphorylation of the CrkII adaptor protein modulates cell migration
http://hdl.handle.net/2297/29264
http://hdl.handle.net/2297/29264ff5016ea-aa4c-415c-beb6-52e370a6cd09
名前 / ファイル | ライセンス | アクション |
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CA-PR-TAKINO-T-3145.pdf (811.5 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2017-10-05 | |||||
タイトル | ||||||
タイトル | Tyrosine phosphorylation of the CrkII adaptor protein modulates cell migration | |||||
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 |
Takino, Takahisa
× Takino, Takahisa× Tamura, Masahito× Miyamori, Hisashi× Araki, Masaru× Matsumoto, Kazue× Sato, Hiroshi× Yamada, Kenneth M. |
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書誌情報 |
Journal of Cell Science 巻 116, 号 15, p. 3145-3155, 発行日 2003-08-01 |
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ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0021-9533 | |||||
NCID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA00694823 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1242/jcs.00632 | |||||
出版者 | ||||||
出版者 | Company of Biologists | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | CrkII belongs to a family of adaptor proteins that become tyrosine phosphorylated after various stimuli. We examined the role of CrkII tyrosine phosphorylation in fibronectin-induced cell migration. Overexpression of CrkII inhibited dephosphorylation of focal adhesion components such as p130 Crk-associated substrate (p130cas) and paxillin by protein tyrosine phosphatase 1B (PTP1B). Tyrosine-phosphorylated CrkII was dephosphorylated by PTP1B both in vitro and in vivo, showing for the first time that PTP1B directly dephosphorylates CrkII. A CrkII mutant in which tyrosine residue 221 was substituted by phenylalanine (CrkII-Y221F) could not be tyrosine phosphorylated, and it showed significantly increased binding to p130cas and paxillin. Enhanced binding of CrkII to p130cas has been reported to promote cell migration. Nonphosphorylated CrkII-Y221F promoted HT1080 cell migration on fibronectin, whereas wild-type CrkII did not at moderate expression levels. Moreover, co-expression of CrkII and PTP1B promoted HT1080 cell migration on fibronectin and retained tyrosine phosphorylation and binding of p130cas to CrkII, whereas paxillin tyrosine phosphorylation was reduced. These findings support the concepts that CrkII binding activity is regulated by tyrosine kinases and phosphatases, and that tyrosine phosphorylation of CrkII can downmodulate cell migration mediated by the focal adhesion kinase/p130cas pathway. | |||||
権利 | ||||||
権利情報 | © The Company of Biologists Limited 2003 | |||||
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 | |||||
関連URI | ||||||
識別子タイプ | URI | |||||
関連識別子 | http://jcs.biologists.org/content/116/15/3145 |