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

Research output: Contribution to journalArticle

22 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)238-251
Number of pages14
JournalEuropean Journal of Cell Biology
Volume93
Issue number5-6
DOIs
Publication statusPublished - 2014

Fingerprint

Actin Depolymerizing Factors
Actin Cytoskeleton
Actins
Protein Domains
Proteins

Keywords

  • Actin
  • ADF-H domain
  • ADF/cofilin
  • Conformational dynamics
  • Cytoskeleton
  • Nucleotide

ASJC Scopus subject areas

  • Cell Biology
  • Histology
  • Pathology and Forensic Medicine
  • Medicine(all)

Cite this

The other side of the coin : Functional and structural versatility of ADF/cofilins. / Hild, G.; Kalmár, L.; Kardos, Roland; Nyitrai, M.; Bugyi, B.

In: European Journal of Cell Biology, Vol. 93, No. 5-6, 2014, p. 238-251.

Research output: Contribution to journalArticle

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