Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization
Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization
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DOI：
10.1006/bbrc.1997.8064
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发表时间：
1998-02-04
影响因子：
3.1
通讯作者：
Takenawa, T
中科院分区：
文献类型：
--
作者：
Miki, H;Takenawa, T
Verprolin 是一种酵母蛋白，其失活导致细胞骨架缺陷，其特征是肌动蛋白丝的异常组织。最近，两种先前显示调节肌动蛋白细胞骨架的哺乳动物蛋白，Wiskott-Aldrich 综合征蛋白（WASP）及其在神经元中表达的同源物（N-WASP），被发现具有与 Verprolin 的一部分同源的短肽基序，然而，同源区域（verprolin-同源结构域， VPH 域）仍然未知。在这里，我们报告了 VPH 结构域作为直接肌动蛋白结合区域的重要性。就 N-WASP 而言，VPH 结构域与丝切蛋白同源区域共同作用，在体外切断肌动蛋白丝。此外，VPH结构域对于活细胞中酪氨酸激酶下游的N-WASP重组肌动蛋白细胞骨架是不可或缺的。所有数据都表明VPH结构域在肌动蛋白细胞骨架的调节中起着关键作用。 (C) 1998 年学术出版社。
Verprolin is a yeast protein whose inactivation leads to a cytoskeletal defect characterized by the abnormal organization of actin filaments, Recently, two mammalian proteins previously shown to regulate the actin cytoskeleton, Wiskott-Aldrich Syndrome Protein (WASP) and its homolog expressed in neurons (N-WASP), were found to possess short peptide motifs homologous to one part of verprolin, However, the physiological function of the homologous regions (verprolin-homology domain, VPH domain) remains unknown. Here we report the importance of the VPH domain as the direct actin binding region. In the case of N-WASP, the VPH domain co-acts with the cofilin-homologous region to sever actin filaments in vitro. Furthermore, the VPH domain is indispensable for the reorganization of the actin cytoskeleton by N-WASP downstream of tyrosine kinases in living cells, All data demonstrate that the VPH domain plays critical roles in the regulation of the actin cytoskeleton. (C) 1998 Academic Press.