The other side of the coin: functional and structural versatility of ADF/cofilins.
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.
University of Pécs, Medical School, Department of Biophysics, Szigeti str. 12, H-7624 Pécs, Hungary; Szentágothai Research Center, Ifjúság str. 34, H-7624 Pécs, Hungary.
Gábor
G
Hild
Institute of Enzymology, Hungarian Academy of Sciences, Research Centre for Natural Sciences, PO Box 7, H-1518 Budapest, Hungary.
Lajos
L
Kalmár
University of Pécs, Medical School, Department of Biophysics, Szigeti str. 12, H-7624 Pécs, Hungary; Szentágothai Research Center, Ifjúság str. 34, H-7624 Pécs, Hungary.
Roland
R
Kardos
University of Pécs, Medical School, Department of Biophysics, Szigeti str. 12, H-7624 Pécs, Hungary; Szentágothai Research Center, Ifjúság str. 34, H-7624 Pécs, Hungary; MTA-PTE Nuclear and Mitochondrial Interactions Research Group, Hungarian Academy of Sciences, Office for Subsidized Research Units, Nádor str. 7, H-1051 Budapest, Hungary.
Miklós
M
Nyitrai
University of Pécs, Medical School, Department of Biophysics, Szigeti str. 12, H-7624 Pécs, Hungary; Szentágothai Research Center, Ifjúság str. 34, H-7624 Pécs, Hungary. Electronic address: beata.bugyi@aok.pte.hu.
Beáta
B
Bugyi
D008841:Actin Cytoskeleton / Q000378:metabolism; D051339:Actin Depolymerizing Factors / Q000737:chemistry* / Q000378:metabolism*; D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary
D051339:Actin Depolymerizing Factors; D000199:Actins
ADF-H domain; ADF/cofilin; Actin; Conformational dynamics; Cytoskeleton; Nucleotide