FEBS Letters | |
Does Vav bind to F‐actin through a CH domain? | |
Castresana, Jose1  Saraste, Matti1  | |
[1] European Molecular Biology Laboratory, Postfach 102209, D-69012 Heidelberg, Germany | |
关键词: Calponin-homology; Cytoskeleton; Signal transduction; Vav; Actin binding; | |
DOI : 10.1016/0014-5793(95)01098-Y | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
An actin-binding protein domain we call here ‘calponin-homology’ or CH is present in signalling proteins such as Vav which are involved in activation and inactivation of small G-proteins. Using profile methods, we have detected two repeats of this domain in the actin-binding region of α-actinin and related proteins. Based on this, we propose that CH domain in Vav and other signalling proteins is employed for association with filamentous actin, and that this function correlates with their control on the G-proteins Rac and Rho which are involved in the organization of cytoskeleton.
【 授权许可】
Unknown
【 预 览 】
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