Domain movement in gelsolin: A calcium-activated switch

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

doi:10.1126/science.286.5446.1939

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 journal › Article › peer-review

134 Scopus citations

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 language	English (US)
Pages (from-to)	1939-1942
Number of pages	4
Journal	Science
Volume	286
Issue number	5446
DOIs	https://doi.org/10.1126/science.286.5446.1939
State	Published - Dec 3 1999

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title = "Domain movement in gelsolin: A calcium-activated switch",

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.",

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T2 - A calcium-activated switch

AU - Robinson, Robert C.

AU - Mejillano, Marisan

AU - Le, Vincent P.

AU - Burtnick, Leslie D.

AU - Yin, Helen L.

AU - Choe, Senyon

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AB - 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.

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Domain movement in gelsolin: A calcium-activated switch

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