WEKO3
アイテム
Effects of Halogenation on Tyrosine Phosphorylation and Peptide Binding to the Src Homology 2 Domain of Lymphocyte-Specific Protein Tyrosine Kinase
https://repo.qst.go.jp/records/46273
https://repo.qst.go.jp/records/46273ca4d6c9e-8960-4067-80d9-a9b106c52027
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2012-02-24 | |||||
| タイトル | ||||||
| タイトル | Effects of Halogenation on Tyrosine Phosphorylation and Peptide Binding to the Src Homology 2 Domain of Lymphocyte-Specific Protein Tyrosine Kinase | |||||
| 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 | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
Okamura, Toshimitsu
× Okamura, Toshimitsu× Kikuchi, Tatsuya× Nodaira, Mika× Odaka, Kenichi× Fukushi, Kiyoshi× Irie, Toshiaki× 岡村 敏充× 菊池 達矢× 野平 美佳× 小高 謙一× 福士 清× 入江 俊章 |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Phosphorylation of tyrosine residues by protein tyrosine kinases (PTK) and phosphotyrosine/Src homology 2 (SH2) domain interactions are crucial not only for signal transduction but also for regulation of PTK activity. Tyrosine residues also receive nitration and halogenation under oxidative conditions. It has been reported that nitration of tyrosine residue caused peptides to be a poor substrate for PTK and that nitrotyrosine residues could bind to SH2 domains as a phosphotyrosine mimic to activate Src family kinase. However, the effect of halogenation on tyrosine phosphorylation or SH2 domain binding is not well understood. We examined the phosphorylation of model peptides containing 3-halotyrosine or 3-nitrotyrosine using typical receptor and nonreceptor tyrosine kinase (EGFR and Lck, respectively). The EGFR- and Lck-mediated phosphorylation was markedly inhibited by tyrosine halogenation. Iodination showed the strongest inhibition of the phosphorylation among four types of halogenation, and its inhibitory effect was stronger than that of nitration. We also examined the effect of iodination and nitration of tyrosine residues on binding to the SH2 domain of Lck, using a model peptide containing the phosphoTyr-Glu-Glu-Ile motif, which has a high affinity for the SH2 domain. The relative affinities of the modified peptides whose phosphotyrosine was substituted with unphosphorylated tyrosine, 3-nitrotyrosine, and 3-iodotyrosine, and of the model peptide were 0.024, 0.26, 1, and 16, respectively. These results suggest that tyrosine iodination may have an effect on the phosphorylation or binding to the SH2 domain similar to nitration. Tyrosine iodination possibly modulates signal transduction, with the potential impairment of cell function. |
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| 書誌情報 |
Biological & Pharmaceutical Bulletin 巻 35, 号 3, p. 433-437, 発行日 2012-03 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0918-6158 | |||||
