Characterization of interaction between CLP36 and palladin
Characterization of interaction between CLP36 and palladin
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DOI：
10.1111/j.1742-4658.2009.07001.x
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发表时间：
2009-05-01
期刊：
影响因子：
5.4
通讯作者：
Senga, Takeshi
中科院分区：
文献类型：
--
作者：
Maeda, Masao;Asano, Eri;Senga, Takeshi
CLP36是PDZ-Lim蛋白家族的一员，与α-肌动蛋白结合，定位于肌动蛋白细胞骨架。CLP36参与了应力纤维和局灶性粘连的形成；然而，CLP36如何调控应力纤维形成的分子机制尚不清楚。为了研究CLP36的生理功能，我们进行了酵母双杂交筛选，发现CLP36与Palladin相互作用。Palladin是肌动蛋白细胞骨架的重要结构元素，广泛表达并与α-肌动蛋白相关。这种相互作用依赖于CLP36的PDZ结构域和Palladin的C末端，沉默Palladin抑制了CLP36对应力纤维的定位。CLP36的PDZ结构域的过表达也抑制了Palladin在应激纤维上的定位，这表明CLP36和Palladin的结合对于这两种蛋白在应激纤维上的定位是重要的。我们的实验结果表明，α-肌动蛋白、CLP36和Palladin形成了一个蛋白质复合体，有助于肌动蛋白细胞骨架的调节。
CLP36 is a member of the PDZ-LIM family of proteins, which associates with alpha-actinin and localizes to the actin cytoskeleton. CLP36 is involved in the formation of stress fibers and focal adhesions; however, the molecular mechanism of how CLP36 regulates stress fiber formation is still unknown. To investigate the physiological function of CLP36, we performed yeast two-hybrid screening, and found that CLP36 interacts with palladin. Palladin is an important structural element of the actin cytoskeleton that is ubiquitously expressed and associates with alpha-actinin. The interaction was dependent on the PDZ domain of CLP36 and the C-terminus of palladin, and silencing of palladin suppressed localization of CLP36 to stress fibers. Overexpression of the PDZ domain of CLP36 also inhibited the localization of palladin to stress fibers, suggesting that the association of CLP36 and palladin is important for the localization of both proteins to stress fibers. Our experimental results indicate that alpha-actinin, CLP36 and palladin form a protein complex and contribute to regulation of the actin cytoskeleton.