Structure of arp2/3 complex in its activated state and in actin filament branch junctions

N. Volkmann; K. J. Amann; S. Stoilova-McPhie; C. Egile; D. C. Winter; L. Hazelwood; J. E. Heuser; R. Li; T. D. Pollard; D. Hanein

doi:10.1126/science.1063025

Structure of arp2/3 complex in its activated state and in actin filament branch junctions

N. Volkmann, K. J. Amann, S. Stoilova-McPhie, C. Egile, D. C. Winter, L. Hazelwood, J. E. Heuser, R. Li, T. D. Pollard, D. Hanein

Research output: Contribution to journal › Article › peer-review

192 Scopus citations

Abstract

The seven-subunit Arp2/3 complex choreographs the formation of branched actin networks at the leading edge of migrating cells. When activated by Wiskott-Aldrich Syndrome protein (WASp), the Arp2/3 complex initiates actin filament branches from the sides of existing filaments. Electron cryomicroscopy and three-dimensional reconstruction of Acanthamoeba castellanii and Saccharomyces cerevisiae Arp2/3 complexes bound to the WASp carboxy-terminal domain reveal asymmetric, oblate ellipsoids. Image analysis of actin branches indicates that the complex binds the side of the mother filament, and Arp2 and Arp3 (for actin-related protein) are the first two subunits of the daughter filament. Comparison to the actin-free, WASp-activated complexes suggests that branch initiation involves large-scale structural rearrangements within Arp2/3.

Original language	English (US)
Pages (from-to)	2456-2459
Number of pages	4
Journal	Science
Volume	293
Issue number	5539
DOIs	https://doi.org/10.1126/science.1063025
State	Published - Sep 28 2001
Externally published	Yes

ASJC Scopus subject areas

General

Access to Document

10.1126/science.1063025

Cite this

@article{c318129fff244d70b9eb7d9b5a2c8663,

title = "Structure of arp2/3 complex in its activated state and in actin filament branch junctions",

abstract = "The seven-subunit Arp2/3 complex choreographs the formation of branched actin networks at the leading edge of migrating cells. When activated by Wiskott-Aldrich Syndrome protein (WASp), the Arp2/3 complex initiates actin filament branches from the sides of existing filaments. Electron cryomicroscopy and three-dimensional reconstruction of Acanthamoeba castellanii and Saccharomyces cerevisiae Arp2/3 complexes bound to the WASp carboxy-terminal domain reveal asymmetric, oblate ellipsoids. Image analysis of actin branches indicates that the complex binds the side of the mother filament, and Arp2 and Arp3 (for actin-related protein) are the first two subunits of the daughter filament. Comparison to the actin-free, WASp-activated complexes suggests that branch initiation involves large-scale structural rearrangements within Arp2/3.",

author = "N. Volkmann and Amann, {K. J.} and S. Stoilova-McPhie and C. Egile and Winter, {D. C.} and L. Hazelwood and Heuser, {J. E.} and R. Li and Pollard, {T. D.} and D. Hanein",

year = "2001",

month = sep,

day = "28",

doi = "10.1126/science.1063025",

language = "English (US)",

volume = "293",

pages = "2456--2459",

journal = "Science",

issn = "0036-8075",

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

number = "5539",

}

TY - JOUR

T1 - Structure of arp2/3 complex in its activated state and in actin filament branch junctions

AU - Volkmann, N.

AU - Amann, K. J.

AU - Stoilova-McPhie, S.

AU - Egile, C.

AU - Winter, D. C.

AU - Hazelwood, L.

AU - Heuser, J. E.

AU - Li, R.

AU - Pollard, T. D.

AU - Hanein, D.

PY - 2001/9/28

Y1 - 2001/9/28

N2 - The seven-subunit Arp2/3 complex choreographs the formation of branched actin networks at the leading edge of migrating cells. When activated by Wiskott-Aldrich Syndrome protein (WASp), the Arp2/3 complex initiates actin filament branches from the sides of existing filaments. Electron cryomicroscopy and three-dimensional reconstruction of Acanthamoeba castellanii and Saccharomyces cerevisiae Arp2/3 complexes bound to the WASp carboxy-terminal domain reveal asymmetric, oblate ellipsoids. Image analysis of actin branches indicates that the complex binds the side of the mother filament, and Arp2 and Arp3 (for actin-related protein) are the first two subunits of the daughter filament. Comparison to the actin-free, WASp-activated complexes suggests that branch initiation involves large-scale structural rearrangements within Arp2/3.

AB - The seven-subunit Arp2/3 complex choreographs the formation of branched actin networks at the leading edge of migrating cells. When activated by Wiskott-Aldrich Syndrome protein (WASp), the Arp2/3 complex initiates actin filament branches from the sides of existing filaments. Electron cryomicroscopy and three-dimensional reconstruction of Acanthamoeba castellanii and Saccharomyces cerevisiae Arp2/3 complexes bound to the WASp carboxy-terminal domain reveal asymmetric, oblate ellipsoids. Image analysis of actin branches indicates that the complex binds the side of the mother filament, and Arp2 and Arp3 (for actin-related protein) are the first two subunits of the daughter filament. Comparison to the actin-free, WASp-activated complexes suggests that branch initiation involves large-scale structural rearrangements within Arp2/3.

UR - http://www.scopus.com/inward/record.url?scp=0035964794&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035964794&partnerID=8YFLogxK

U2 - 10.1126/science.1063025

DO - 10.1126/science.1063025

M3 - Article

C2 - 11533442

AN - SCOPUS:0035964794

SN - 0036-8075

VL - 293

SP - 2456

EP - 2459

JO - Science

JF - Science

IS - 5539

ER -

Structure of arp2/3 complex in its activated state and in actin filament branch junctions

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this