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Updated: Apr 29, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
Published on: July 30, 2014
The other side of the coin: functional and structural versatility of ADF/cofilins
Gábor Hild1, Lajos Kalmár2, Roland Kardos1
1University of Pécs, Medical School, Department of Biophysics, Szigeti str. 12, H-7624 Pécs, Hungary; Szentágothai Research Center, Ifjúság str. 34, H-7624 Pécs, Hungary.
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.
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