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- W2030159892 abstract "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 Fcɛ receptor (FcɛR), in microbial motility and in Syk protein stability." @default.
- W2030159892 created "2016-06-24" @default.
- W2030159892 creator A5036390677 @default.
- W2030159892 creator A5043034701 @default.
- W2030159892 date "2006-04-01" @default.
- W2030159892 modified "2023-09-27" @default.
- W2030159892 title "WIP: A multifunctional protein involved in actin cytoskeleton regulation" @default.
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- W2030159892 doi "https://doi.org/10.1016/j.ejcb.2005.08.004" @default.
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