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 journalArticle

128 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1939-1942
Number of pages4
JournalScience
Volume286
Issue number5446
DOIs
Publication statusPublished - Dec 3 1999
Externally publishedYes

ASJC Scopus subject areas

  • General

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    Robinson, R. C., Mejillano, M., Le, V. P., Burtnick, L. D., Yin, H. L., & Choe, S. (1999). Domain movement in gelsolin: A calcium-activated switch. Science, 286(5446), 1939-1942. https://doi.org/10.1126/science.286.5446.1939