Antón Inés M, Jones Gareth E
Centro de Biología Molecular Severo Ochoa CSIC-UAM, Facultad de Ciencias, Campus UAM, Cantoblanco, E-28049 Madrid, Spain.
Eur J Cell Biol. 2006 Apr;85(3-4):295-304. doi: 10.1016/j.ejcb.2005.08.004. Epub 2005 Sep 19.
Knowledge of the dynamics of actin-based structures is a major key to understanding how cells move and respond to their environment. The ability to reorganize actin filaments in a spatial and temporal manner to integrate extracellular signals is at the core of cell adhesion and cell migration. Several proteins have been described as regulators of actin polymerization: this review will focus on the role of WASP-interacting protein (WIP), an actin-binding protein that participates in actin polymerization regulation and signal transduction. WIP is widely expressed and interacts with Wiskott-Aldrich syndrome protein (WASP) (a hematopoietic-specific protein) and its more widely expressed homologue neural WASP (N-WASP), to regulate WASP/N-WASP function in Arp2/3-mediated actin polymerization. WIP also interacts with profilin, globular and filamentous actin (G- and F-actin, respectively) and stabilizes actin filaments. In vivo WIP participates in filopodia and lamellipodia formation, in T and B lymphocyte activation, in mast cell degranulation and signaling through the Fcepsilon receptor (FcepsilonR), in microbial motility and in Syk protein stability.
了解基于肌动蛋白的结构动态是理解细胞如何移动以及如何对环境做出反应的关键所在。以时空方式重组肌动蛋白丝以整合细胞外信号的能力是细胞黏附和细胞迁移的核心。已有几种蛋白质被描述为肌动蛋白聚合的调节因子：本综述将聚焦于WASP相互作用蛋白（WIP）的作用，它是一种肌动蛋白结合蛋白，参与肌动蛋白聚合调节和信号转导。WIP广泛表达，并与威斯科特-奥尔德里奇综合征蛋白（WASP，一种造血特异性蛋白）及其更广泛表达的同源物神经WASP（N-WASP）相互作用，以调节WASP/N-WASP在Arp2/3介导的肌动蛋白聚合中的功能。WIP还与肌动蛋白 Profilin、球状和丝状肌动蛋白（分别为G-肌动蛋白和F-肌动蛋白）相互作用，并稳定肌动蛋白丝。在体内，WIP参与丝状伪足和片状伪足的形成、T和B淋巴细胞的激活、肥大细胞的脱颗粒以及通过Fcepsilon受体（FcepsilonR）的信号传导、微生物运动以及Syk蛋白的稳定性。
