Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal adhesion adaptor proteins paxillin and Hic-5
Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal adhesion adaptor proteins paxillin and Hic-5
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DOI：
10.1074/jbc.m110291200
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发表时间：
2002-04-05
影响因子：
4.8
通讯作者：
Goetinck, PF
中科院分区：
文献类型：
--
作者：
Denhez, F;Wilcox-Adelman, SA;Goetinck, PF
Syndecan-4和整合素是细胞黏附于细胞外基质分子的局灶黏附的主要跨膜受体。Syndesmos是一种细胞质蛋白，与syndecan-4的细胞质结构域特异性相互作用，并在局灶接触中与syndecan-4共定位。在本研究中，我们寻找可能与综合征相互作用的因素。我们发现该综合征与局灶黏附接头蛋白paxillin相互作用。syndesmos与paxillin的结合是直接的，这些相互作用是由蛋白激酶c的激活触发的。syndesmos还与paxillin同源物Hic-5结合。syndecan-4通过联desmos与paxillin的连接与paxillin与整合素的连接相似，因此可能反映了这两种受体在局灶粘连和肌动蛋白应激纤维组装中的协同信号传导。
Syndecan-4 and integrins are the primary transmembrane receptors of focal adhesions in cells adherent to extracellular matrix molecules. Syndesmos is a cytoplasmic protein that interacts specifically with the cytoplasmic domain of syndecan-4, and it co-localizes with syndecan-4 in focal contacts. In the present study we sought possible interactors with syndesmos. We find that syndesmos interacts with the focal adhesion adaptor protein paxillin. The binding of syndesmos to paxillin is direct, and these interactions are triggered by the activation of protein kinase C. Syndesmos also binds the paxillin homolog, Hic-5. The connection of syndecan-4 with paxillin through syndesmos parallels the connection between paxillin and integrins and may thus reflect the cooperative signaling of these two receptors in the assembly of focal adhesions and actin stress fibers.