Domain movement in gelsolin: A calcium-activated switch

Robert C. Robinson, Marisan Mejillano, Vincent P. Le, Leslie D. Burtnick, Helen L. Yin, Senyon Choe

Research output: Contribution to journalArticlepeer-review

134 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1939-1942
Number of pages4
Issue number5446
StatePublished - Dec 3 1999

ASJC Scopus subject areas

  • General


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