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

Trends Cell Biol. 2007 Nov;17(11):555-62. doi: 10.1016/j.tcb.2007.08.005. Epub 2007 Oct 18.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actins / metabolism
  • Animals
  • Cytoskeletal Proteins / chemistry*
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism*
  • Cytoskeletal Proteins / physiology
  • Humans
  • Intracellular Signaling Peptides and Proteins / chemistry*
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Intracellular Signaling Peptides and Proteins / physiology
  • Protein Processing, Post-Translational* / genetics
  • Protein Transport / genetics
  • Protein Transport / physiology
  • Wiskott-Aldrich Syndrome Protein / chemistry*
  • Wiskott-Aldrich Syndrome Protein / genetics
  • Wiskott-Aldrich Syndrome Protein / metabolism*
  • Wiskott-Aldrich Syndrome Protein / physiology

Substances

  • Actins
  • Cytoskeletal Proteins
  • Intracellular Signaling Peptides and Proteins
  • WIPF1 protein, human
  • Wiskott-Aldrich Syndrome Protein