β2-Chimaerin binds to EphA receptors and regulates cell migration
β2-Chimaerin binds to EphA receptors and regulates cell migration
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DOI：
10.1016/j.febslet.2009.03.032
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发表时间：
2009-04-17
期刊：
影响因子：
3.5
通讯作者：
Katoh, Hironori
中科院分区：
文献类型：
--
作者：
Takeuchi, Shingo;Yamaki, Nao;Katoh, Hironori
Ephrin和Eph受体在发育过程中调节细胞迁移中起关键作用。我们发现，RacGAP β 2-嵌合蛋白（嵌合蛋白）结合EphA 2和EphA 4，并灭活Rac 1响应ephrinA 1刺激。EphA 4通过其激酶结构域与β 2-嵌合蛋白结合，并促进Rac 1与β 2-嵌合蛋白的结合。此外，内源性β 2-嵌合蛋白的敲低阻断了ephrinA 1诱导的细胞迁移抑制。这些结果表明，β 2-嵌合蛋白被EphA受体激活，并介导细胞迁移的EphA受体依赖性调节。
Ephrins and Eph receptors have key roles in regulation of cell migration during development. We found that the RacGAP beta 2-chimaerin (chimerin) bound to EphA2 and EphA4 and inactivated Rac1 in response to ephrinA1 stimulation. EphA4 bound to beta 2-chimaerin through its kinase domain and promoted binding of Rac1 to beta 2-chimaerin. In addition, knockdown of endogenous beta 2-chimaerin blocked ephrinA1-induced suppression of cell migration. These results suggest that beta 2-chimaerin is activated by EphA receptors and mediates the EphA receptor-dependent regulation of cell migration.