The gelsolin family of actin regulatory proteins: modular structures, versatile functions.
This issue of FEBS Letters includes two manuscripts describing structural studies of gelsolin, the best-characterized member of a superfamily of actin binding proteins that sever, cap, and in some cases nucleate and bundle actin filaments. The manuscripts by Narayan et al. and Irobi et al. provide snapshots of gelsolin domains activated by calcium and in complex with the actin monomer, revealing new insights into the remarkable actin regulatory activities of this versatile protein. These studies build upon nearly a quarter of a century of research on gelsolin's effects on actin dynamics and its role in normal and diseased cells. In the following minireview, we summarize the structural studies that have provided insights into gelsolin's severing and capping activities and look to the future of work on this remarkable molecule.
McGough
Amy M
AM
Markey Center for Structural Biology, Purdue University, West Lafayette, IN 47907-1392, USA. mcgougha@purdue.edu
Staiger
Chris J
CJ
Min
Jung Ki
JK
Simonetti
Karen D
KD
D000199:Actins / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000378:metabolism; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D018260:Gelsolin / Q000737:chemistry* / Q000502:physiology*; D006801:Humans; D008958:Models, Molecular; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D000199:Actins; D018260:Gelsolin; D002118:Calcium