Cortactin interacts with WIP in regulating arp2/3 activation and membrane protrusion
Cortactin interacts with WIP in regulating arp2/3 activation and membrane protrusion
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DOI：
10.1016/s0960-9822(03)00107-6
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发表时间：
2003-03-04
期刊：
影响因子：
9.2
通讯作者：
Parsons, JT
中科院分区：
文献类型：
--
作者：
Kinley, AW;Weed, SA;Parsons, JT
背景：肌动蛋白细胞骨架组装的调节是许多细胞事件中不可或缺的一步。肌动蛋白聚合的关键调节因子是Arp 2/3复合物。结果：通过酵母双杂交筛选，证实了Corp 3结构域与WASP相互作用蛋白（WASP Interacting Protein，WASP）的一段cDNA片段的相互作用。GST-coronin相互作用与SH 3依赖的方式。coronin和coronin的亚细胞定位在细胞周边一致。α-葡聚糖以浓度依赖性方式增加皮质素介导的Arp 2/3复合物激活肌动蛋白聚合的效率。最后，corneum和corneum的共表达刺激膜projections.Conclusions：corneum，一种参与丝状伪足形成的蛋白质，结合到肌动蛋白单体和corneum。因此，将肌动蛋白单体募集到皮质素激活的Arp 2/3复合物中可能导致观察到的Cortactin激活Arp 2/3复合物的增加。这些数据表明，皮质素-肌动蛋白复合物的功能，在调节肌动蛋白为基础的结构在细胞周边。
Background: Modulation of actin cytoskeleton assembly is an integral step in many cellular events. A key regulator of actin polymerization is Arp2/3 complex. Cortactin, an F-actin binding protein that localizes to membrane ruffles, is an activator of Arp2/3 complex.Results: A yeast two-hybrid screen revealed the interaction of the cortactin Src homology 3 (SH3) domain with a peptide fragment derived from a cDNA encoding a region of WASp-Interacting Protein (WIP). GST-cortactin interacted with WIP in an SH3-dependent manner. The subcellular localization of cortactin and WIP coincided at the cell periphery. WIP increased the efficiency of cortactin-mediated Arp2/3 complex activation of actin polymerization in a concentration-dependent manner. Lastly, coexpression of cortactin and WIP stimulated membrane protrusions.Conclusions: WIP, a protein involved in filopodia formation, binds to both actin monomers and cortactin. Thus, recruitment of actin monomers to a cortactin-activated Arp2/3 complex likely leads to the observed increase in cortactin activation of Arp2/3 complex by WIP. These data suggest that a cortactin-WIP complex functions in regulating actin-based structures at the cell periphery.