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

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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

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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",

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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.

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SP - 2456

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JO - Science

JF - Science

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ER -

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

Abstract

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