Research & Teaching Faculty

Default Header Image

Domain movement in gelsolin: A calcium-activated switch

TitleDomain movement in gelsolin: A calcium-activated switch
Publication TypeJournal Article
Year of Publication1999
AuthorsRobinson, RC, Mejillano, M, Le, VP, Burtnick, LD, Yin, HL, Choe, S
JournalScience
Volume286
Pagination1939-1942
Date PublishedDec
Type of ArticleArticle
ISBN Number0036-8075
Keywordsactin, BINDING-SITE, COMPLEX, FILAMENT, IDENTIFICATION, PLASMA GELSOLIN
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 beta sheet core of G4 and G6. This exposes the actin-binding site on G4, enabling severing and capping of actin filaments to proceed.

URL<Go to ISI>://000084003400047