Spire and Cordon-bleu: multifunctional regulators of actin dynamics

Trends Cell Biol. 2008 Oct;18(10):494-504. doi: 10.1016/j.tcb.2008.07.008. Epub 2008 Sep 5.

Abstract

WASP-homology 2 (WH2) domains, which were first identified in the WASP/Scar (suppressor of cAMP receptor)/WAVE (WASP-family verprolin homologous protein) family of proteins, are multifunctional regulators of actin assembly. Two recently discovered actin-binding proteins, Spire and Cordon-bleu (Cobl), which have roles in axis patterning in developmental processes, use repeats of WH2 domains to generate a large repertoire of novel regulatory activities, including G-actin sequestration, actin-filament nucleation, filament severing and barbed-end dynamics regulation. We describe how these multiple functions selectively operate in a cellular context to control the dynamics of the actin cytoskeleton. In vivo, Spire and Cobl can synergize with other actin regulators. As an example, we outline potential methods to gain insight into the functional basis for reported genetic interactions among Spire, profilin and formin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actin-Related Protein 2-3 Complex / metabolism*
  • Actins / metabolism*
  • Animals
  • Cytoskeletal Proteins
  • Cytoskeleton / metabolism
  • Mice
  • Profilins / metabolism*
  • Proteins / metabolism*
  • Thymosin / metabolism
  • Wiskott-Aldrich Syndrome Protein Family / metabolism*

Substances

  • Actin-Related Protein 2-3 Complex
  • Actins
  • Cobl protein, mouse
  • Cytoskeletal Proteins
  • Profilins
  • Proteins
  • Wiskott-Aldrich Syndrome Protein Family
  • Thymosin