Role of interaction with vinculin in recruitment of vinexins to focal adhesions.

Role of interaction with vinculin in recruitment of vinexins to focal adhesions.
复制标题

DOI:
10.1016/j.bbrc.2005.08.064
复制
发表时间:
2005-10
影响因子:
3.1
通讯作者:
H. Takahashi;Masaru Mitsushima;N. Okada;Takuya Ito;Sanae Aizawa;Rie Akahane;Tsutomu Umemoto;K. Ueda;N. Kioka
H. Takahashi;Masaru Mitsushima;N. Okada;Takuya Ito;Sanae Aizawa;Rie Akahane;Tsutomu Umemoto;K. Ueda;N. Kioka
中科院分区:
生物学4区
文献类型:
--
作者:
H. Takahashi;Masaru Mitsushima;N. Okada;Takuya Ito;Sanae Aizawa;Rie Akahane;Tsutomu Umemoto;K. Ueda;N. Kioka

文献摘要

相似文献

尽管vinexin最初被鉴定为与黏着斑蛋白的富含脯氨酸的铰链区结合的蛋白质,但vinexin-黏着斑蛋白相互作用的功能和生化性质尚不清楚。在这里,我们使用表面等离子体共振测量确定了vinexin-vinculin相互作用的亲和力,并发现vinexin β与vinculin的C-末端一半相互作用,其模拟活化的“开放”形式,亲和力比全长“封闭”vinculin高三倍。免疫共沉淀实验表明,纤维连接蛋白上的细胞粘附增强了vinexin-vinculin的相互作用。我们还表明,与黏着斑蛋白的相互作用是必要的有效定位的vinexin α和β在局灶性粘连。这些观察结果表明,“激活”黏着斑蛋白定位于粘着斑的模型将黏着斑蛋白募集到粘着斑。
Although vinexin was originally identified as a protein binding to the proline-rich hinge region of vinculin, the functions and biochemical properties of the vinexin–vinculin interaction are not known. Here, we determined the affinity of the vinexin–vinculin interaction using surface plasmon resonance measurements and found that vinexin β interacts with the C-terminal half of vinculin, which mimics an activated “open” form, with a threefold higher affinity than with the full-length “closed” vinculin. Coimmunoprecipitation experiments showed that cell adhesion on fibronectin enhances the vinexin–vinculin interaction. We also show that the interaction with vinculin is necessary for the efficient localization of vinexin α and β at focal adhesions. These observations suggest a model that “activated” vinculin localized at focal adhesions recruits vinexins to focal adhesions.