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Trends Cell Biol. 2007 Nov;17(11):555-62. Epub 2007 Oct 18.

WASP-interacting protein (WIP): working in polymerisation and much more.

Author information

1
Centro de Biología Molecular Severo Ochoa, CSIC-UAM, Facultad de Ciencias, Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain. ianton@cbm.uam.es

Abstract

The migration of cells and the movement of some intracellular pathogens, such as Shigella and Vaccinia, are dependent on the actin-based cytoskeleton. Many proteins are involved in regulating the dynamics of the actin-based microfilaments within cells and, among them, WASP and N-WASP have a significant role in the regulation of actin polymerisation. The activity and stability of WASP is regulated by its cellular partner WASP-interacting protein (WIP) during the formation of actin-rich structures, including the immune synapse, filopodia, lamellipodia, stress fibres and podosomes. Here, we review the role of WIP in regulating WASP function by stabilising WASP and shuttling WASP to areas of actin assembly in addition to reviewing the WASP-independent functions of WIP.

PMID:
17949983
DOI:
10.1016/j.tcb.2007.08.005
[Indexed for MEDLINE]

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