Molecular analysis of the interaction between palladin and α-actinin
Molecular analysis of the interaction between palladin and α-actinin
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DOI：
10.1061/j.febslet.2004.04.006
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发表时间：
2004-05-21
期刊：
影响因子：
3.5
通讯作者：
Carpén, O
中科院分区：
文献类型：
--
作者：
Rönty, M;Taivainen, A;Carpén, O
钯金是一种新型的应力纤维致密区成分。反义和短暂过表达研究表明，钯素在肌动蛋白细胞骨架的调控中起重要作用。Palladin colocalizes;而与α -肌动蛋白（一种致密区成分）相互作用的分子细节和功能意义尚未得到研究。我们在这里展示了这两种蛋白之间的直接联系，并在帕拉丁蛋白的短序列和α -肌动蛋白的羧基端钙调蛋白结构域内绘制了结合位点。通过基于转染的靶向实验，我们发现钯金参与了a-肌动蛋白靶向特定亚细胞病灶的过程，这表明两种肌动蛋白相关蛋白之间存在功能相互作用。(C) 2004年欧洲生化学会联合会。Elsevier B.V.版权所有。
Palladin is a novel component of stress fiber dense regions. Antisense and transient overexpression studies have indicated an important role for palladin in the regulation of actin cytoskeleton. Palladin colocalizes; and coinimunoprecipitates with alpha-actinin, a dense region component, but the molecular details and functional significance of the interaction have not been studied. We show here a direct association between the two proteins and have mapped the binding site within a short sequence of palladin and in the carboxy-terminal calmodulin domain of alpha-actinin. Using transfection-based targeting assays, we show that palladin is involved in targeting of a-actinin to specific subcellular foci indicating a functional interplay between the two actin-associated proteins. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.