The gelsolin family of actin regulatory proteins: modular structures, versatile functions

FEBS Letters

Staiger, Chris J¹  Min, Jung-Ki²  Simonetti, Karen D²  McGough, Amy M² 

[1] Department of Biological Sciences, the Purdue Motility Group, Purdue University, West Lafayette, IN 47907-1392, USA;Markey Center for Structural Biology, Purdue University, West Lafayette, IN 47907-1392, USA

关键词: Actin;    Actin binding protein;    Cytoskeleton;    Gelsolin;    Protein structure;    F-actin;    filamentous actin;    EGTA;    ethylene glycol-bis[β-aminoethyl ether]-N;    N;    N′;    N′-tetraacetic acid;    NMR;    nuclear magnetic resonance;    PPI;    polyphosphoinositide;    PIP2;    phosphatidylinositol-4;    5-bisphosphate;   

DOI  :  10.1016/S0014-5793(03)00932-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown