Actin-binding proteins--a unifying hypothesis

Trends Biochem Sci. 2004 Nov;29(11):572-8. doi: 10.1016/j.tibs.2004.09.004.

Abstract

Actin participates in more protein-protein interactions than any other known protein, including the interaction of actin with itself to form the helical polymer F-actin. The vast majority of actin-binding proteins (ABPs) can be grouped into conserved families. Only a handful of structures of complexes of actin with ABPs have been determined so far. These structures are starting to reveal how certain ABPs, including gelsolin, vitamin D-binding protein and Wiskott-Aldrich syndrome protein (WASP)-homology domain-2-related proteins, share a common actin-binding motif. It is proposed here that other ABPs, including actin itself, might share this motif, providing a mechanism whereby ABPs and actin compete for a common binding site. Of particular interest is a hydrophobic pocket that mediates important interactions in five of the existing structures of actin complexes. As the pocket remains accessible in F-actin, it is proposed that this pocket represents a primary target for F-actin-binding proteins, such as calponin-homology-related proteins and myosin.

Publication types

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

MeSH terms

  • Actin Depolymerizing Factors
  • Actins / chemistry*
  • Actins / metabolism
  • Amino Acid Motifs / genetics
  • Amino Acid Sequence
  • Binding Sites / genetics
  • Destrin
  • Drosophila Proteins / chemistry
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism
  • Gelsolin / chemistry
  • Gelsolin / genetics
  • Gelsolin / metabolism
  • Hydrophobic and Hydrophilic Interactions
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism
  • Models, Molecular*
  • Molecular Sequence Data
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism
  • Oxazoles / chemistry
  • Oxazoles / metabolism
  • Protein Binding
  • Protein Conformation
  • Proteins / chemistry
  • Proteins / genetics
  • Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Vitamin D-Binding Protein / chemistry
  • Vitamin D-Binding Protein / genetics
  • Vitamin D-Binding Protein / metabolism
  • Wiskott-Aldrich Syndrome Protein

Substances

  • Actin Depolymerizing Factors
  • Actins
  • Destrin
  • Drosophila Proteins
  • Gelsolin
  • Microfilament Proteins
  • Nerve Tissue Proteins
  • Oxazoles
  • Proteins
  • Vitamin D-Binding Protein
  • Wiskott-Aldrich Syndrome Protein
  • cib protein, Drosophila
  • kabiramide C