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 Re receptor (Fc epsilon R), in microbial motility and in Syk protein stability. (c) 2005 Published by Elsevier GmbH
| Original language | English |
|---|---|
| Pages (from-to) | 295 - 304 |
| Number of pages | 10 |
| Journal | European Journal of Cell Biology |
| Volume | 85 |
| Issue number | 3-4 |
| DOIs | |
| Publication status | Published - 7 Apr 2006 |