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 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 language	English
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
Publication status	Published - Dec 3 1999
Externally published	Yes

ASJC Scopus subject areas

General

Access to Document

10.1126/science.286.5446.1939

Cite this

@article{c33cbc67325d4816b8c34e46cf4f1384,

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.",

author = "Robinson, {Robert C.} and Marisan Mejillano and Le, {Vincent P.} and Burtnick, {Leslie D.} and Yin, {Helen L.} and Senyon Choe",

year = "1999",

month = dec,

day = "3",

doi = "10.1126/science.286.5446.1939",

language = "English",

volume = "286",

pages = "1939--1942",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

number = "5446",

}

TY - JOUR

T1 - Domain movement in gelsolin

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

PY - 1999/12/3

Y1 - 1999/12/3

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=0033521081&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033521081&partnerID=8YFLogxK

U2 - 10.1126/science.286.5446.1939

DO - 10.1126/science.286.5446.1939

M3 - Article

C2 - 10583954

AN - SCOPUS:0033521081

SN - 0036-8075

VL - 286

SP - 1939

EP - 1942

JO - Science

JF - Science

IS - 5446

ER -

Domain movement in gelsolin: A calcium-activated switch

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this