Domain Movement in Gelsolin: A Calcium-Activated Switch
- 3 December 1999
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 286 (5446), 1939-1942
- https://doi.org/10.1126/science.286.5446.1939
Abstract
The actin-binding protein gelsolin is involved in remodeling the actin cytoskeleton during growth-factor signaling, apoptosis, cytokinesis, and cell movement. Calcium-activated gelsolin severs and caps actin filaments. The 3.4 angstrom x-ray structure of the carboxyl-terminal half of gelsolin (G4–G6) in complex with actin reveals the basis for gelsolin activation. Calcium binding induces a conformational rearrangement in which domain G6 is flipped over and translated by about 40 angstroms relative to G4 and G5. The structural reorganization tears apart the continuous β sheet core of G4 and G6. This exposes the actin-binding site on G4, enabling severing and capping of actin filaments to proceed.Keywords
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