WIP: a multifunctional protein involved in actin cytoskeleton regulation |
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Authors: | Antón Inés M Jones Gareth E |
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Affiliation: | Centro de Biología Molecular Severo Ochoa CSIC-UAM, Facultad de Ciencias, Campus UAM, Cantoblanco, E-28049 Madrid, Spain. ianton@cbm.uam.es |
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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 Fcepsilon receptor (FcepsilonR), in microbial motility and in Syk protein stability. |
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Keywords: | WIP WASP N-WASP Arp2/3 Actin cytoskeleton Signal transduction |
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