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WASP/N-WASP相互作用蛋白WIP与肌动蛋白的结合调节粘着斑组装和粘附。

Binding of the WASP/N-WASP-interacting protein WIP to actin regulates focal adhesion assembly and adhesion.

作者信息

Ramesh Narayanaswamy, Massaad Michel J, Kumar Lalit, Koduru Suresh, Sasahara Yoji, Anton Ines, Bhasin Manoj, Libermann Towia, Geha Raif

出版信息

Mol Cell Biol. 2014 Jul;34(14):2600-10. doi: 10.1128/MCB.00017-14.

Abstract

The actin cytoskeleton is essential for cell adhesion and migration, functions important for tumor invasion. In addition to binding N-WASP/WASP, WIP binds and stabilizes F-actin. WIP(-/-) fibroblasts were used to test the role of WIP in F-actin function. WIP(-/-) cells had defective focal adhesion (FA), stress fiber assembly, and adherence to substrates, functions that were restored by transduction of wild-type WIP. Protein and mRNA levels of several FA constituents regulated by the myocardin-related transcription factor (MRTF)–serum response factor (SRF) transcription factor complex were reduced in WIP(-/-) fibroblasts. The level of G-actin, which sequesters MRTF in the cytoplasm, was increased, and nuclear localization of MRTF-A and SRF was reduced, in WIP(-/-) fibroblasts. Transfection of an MRTF-A mutant that constitutively translocates to the nucleus or transfection of constitutively active SRF restored FA and stress fiber assembly. Fibroblasts from knock-in mice expressing a WIP mutant that fails to bind actin phenocopied WIP(-/-) fibroblasts. Thus, WIP is a novel regulator of FA assembly and cell adhesion.

摘要

肌动蛋白细胞骨架对于细胞黏附和迁移至关重要,而细胞黏附和迁移是肿瘤侵袭的重要功能。除了结合N-WASP/WASP外,WIP还能结合并稳定F-肌动蛋白。利用WIP(-/-)成纤维细胞来测试WIP在F-肌动蛋白功能中的作用。WIP(-/-)细胞的粘着斑(FA)、应力纤维组装以及对底物的粘附存在缺陷,而转导野生型WIP可恢复这些功能。在WIP(-/-)成纤维细胞中,由心肌素相关转录因子(MRTF)-血清反应因子(SRF)转录因子复合物调控的几种FA成分的蛋白质和mRNA水平降低。在WIP(-/-)成纤维细胞中,将MRTF隔离在细胞质中的G-肌动蛋白水平升高,MRTF-A和SRF的核定位降低。转染组成型易位至细胞核的MRTF-A突变体或转染组成型活性SRF可恢复FA和应力纤维组装。表达无法结合肌动蛋白的WIP突变体的敲入小鼠的成纤维细胞表现出与WIP(-/-)成纤维细胞相似的表型。因此,WIP是FA组装和细胞黏附的新型调节因子。

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