Journal
EUROPEAN JOURNAL OF CELL BIOLOGY
Volume 85, Issue 3-4, Pages 295-304Publisher
ELSEVIER GMBH, URBAN & FISCHER VERLAG
DOI: 10.1016/j.ejcb.2005.08.004
Keywords
WIP; WASP; N-WASP; Arp2/3; actin cytoskeleton; signal transduction
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Funding
- Wellcome Trust [070613] Funding Source: Medline
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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.
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