The other side of the coin: functional and structural versatility of ADF/cofilins

Eur J Cell Biol. 2014 May-Jun;93(5-6):238-51. doi: 10.1016/j.ejcb.2013.12.001. Epub 2014 Jan 14.

Abstract

Several cellular processes rely on the fine tuning of actin cytoskeleton. A central component in the regulation of this cellular machinery is the ADF-H domain proteins. Despite sharing the same domain, ADF-H domain proteins produce a diverse functional landscape in the regulation of the actin cytoskeleton. Recent findings emphasize that the functional and structural features of these proteins can differ not only between ADF-H families but even within the same family. The structural and evolutional background of this functional diversity is poorly understood. This review focuses on the specific functional characteristics of ADF-H domain proteins and how these features can be linked to structural differences in the ADF-H domain and also to different conformational transitions in actin. In the light of recent discoveries we pay special attention to the ADF/cofilin proteins to find tendencies along which the functional and structural diversification is governed through the evolution.

Keywords: ADF-H domain; ADF/cofilin; Actin; Conformational dynamics; Cytoskeleton; Nucleotide.

Publication types

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

MeSH terms

  • Actin Cytoskeleton / metabolism
  • Actin Depolymerizing Factors / chemistry*
  • Actin Depolymerizing Factors / metabolism*
  • Actins / metabolism
  • Amino Acid Sequence
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary

Substances

  • Actin Depolymerizing Factors
  • Actins