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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >CMS: An adapter molecule involved in cytoskeletal rearrangements
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CMS: An adapter molecule involved in cytoskeletal rearrangements

机译:CMS:参与细胞骨架重排的衔接子分子

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摘要

Cas ligand with multiple Src homology (SH) 3 domains (CMS) is an ubiquitously expressed signal trans- duction molecule that interacts with the focal adhesion protein pl30~Cas. CMS contains three SH3 in its NH_2 terminus and proline-rich sequences in its center region. The latter se- quences mediate the binding to the SH3 domains of p130~Cas, Src-family kinases, p85 subunit of phosphatidylinositol 3-ki- nase, and Grb2. The COOH-terminal region contains putative actin binding sites and a coiled-coil domain that mediates homodimerization of CMS. CMS is a cytoplasmic protein that colocalizes with F-actin and p130~Cas to membrane ruffles and leading edges of cells. Ectopic cxpression of CMS in COS-7 cells resulted in alteration in arrangement of the actin cy- toskeleton. We observed a diffuse distribution of actin in small dots and less actin fiber formation. Altogether, these features suggest that CMS functions as a scaffolding molecule with a specialized role in regulation of the actin cytoskeleton.
机译:具有多个Src同源性(SH)3结构域(CMS)的Cas配体是广泛表达的信号转导分子,它与粘着斑蛋白pl30〜Cas相互作用。 CMS在其NH_2末端包含三个SH3,在其中心区域包含富脯氨酸序列。后者的序列介导了与p130〜Cas,Src家族激酶,磷脂酰肌醇3-激酶的p85亚基和Grb2的SH3结构域的结合。 COOH末端区域包含推定的肌动蛋白结合位点和介导CMS同二聚化的卷曲螺旋结构域。 CMS是一种细胞质蛋白,与F-肌动蛋白和p130〜Cas共定位到膜的褶皱和细胞的前缘。 COS-7细胞中CMS的异位表达导致肌动蛋白细胞骨架排列的改变。我们观察到肌动蛋白在小点中的扩散分布和较少的肌动蛋白纤维形成。总而言之,这些特征表明CMS起着支架分子的作用,在调节肌动蛋白的细胞骨架中起着特殊的作用。

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