Inhibition of RhoA-mediated SRF activation by p116Rip
Inhibition of RhoA-mediated SRF activation by p116Rip
复制标题
DOI：
10.1016/j.febslet.2005.09.083
复制
发表时间：
2005-11-07
期刊：
影响因子：
3.5
通讯作者：
Moolenaar, WH
中科院分区：
文献类型：
--
作者：
Mulder, J;Ariaens, A;Moolenaar, WH
p116（Rip）最初被鉴定为活化RhoA的结合伴侣，是一种肌动蛋白结合蛋白，其与肌球蛋白-II磷酸酶的调节性肌球蛋白结合亚基（MBS）相互作用，并且对于Rho调节的细胞骨架收缩性是必需的。在这里，我们研究了p116（Rip）在RhoA介导的转录因子SRF激活中的作用。我们发现，p116（Rip）寡聚化通过其C-末端卷曲螺旋结构域，当过表达，抑制RhoA诱导的SRF激活，而不影响RhoA-GTP水平。不能寡聚化或结合MBS的p116（Rip）突变形式仍然能够抑制SRF活性。我们的研究结果表明，p116（Rip）干扰RhoA介导的转录，通过其分解的肌动球蛋白细胞骨架下游的RhoA的能力。(c)2005年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
p116(Rip), originally identified as a binding partner of activated RhoA, is an actin-binding protein that interacts with the regulatory myosin-binding subunit (MBS) of myosin-II phosphatase and is essential for Rho-regulated cytoskeletal contractility. Here, we have examined the role of p116(Rip) in RhoA-mediated activation of the transcription factor SRF. We show that p116(Rip) oligomerizes via its C-terminal coiled-coil domain and, when overexpressed, inhibits RhoA-induced SRF activation without affecting RhoA-GTP levels. Mutant forms of p116(Rip) that fail to oligomerize or bind to MBS are still capable of inhibiting SRF activity. Our results suggest that p116(Rip) interferes with RhoA-mediated transcription through its ability to disassemble the actomyosin cytoskeleton downstream of RhoA. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.