The ARP2/3 complex: An actin nucleator comes of age

Erin D. Goley; Matthew D. Welch

doi:10.1038/nrm2026

The ARP2/3 complex: An actin nucleator comes of age

Erin D. Goley
, Matthew D. Welch

Research output: Contribution to journal › Review article › peer-review

615 Scopus citations

Abstract

The cellular functions of the actin cytoskeleton require precise regulation of both the initiation of actin polymerization and the organization of the resulting filaments. The actin-related protein-2/3 (ARP2/3) complex is a central player in this regulation. A decade of study has begun to shed light on the molecular mechanisms by which this powerful machine controls the polymerization, organization and recycling of actin-filament networks, both in vitro and in the living cell.

Original language	English (US)
Pages (from-to)	713-726
Number of pages	14
Journal	Nature Reviews Molecular Cell Biology
Volume	7
Issue number	10
DOIs	https://doi.org/10.1038/nrm2026
State	Published - Oct 23 2006
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1038/nrm2026

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title = "The ARP2/3 complex: An actin nucleator comes of age",

abstract = "The cellular functions of the actin cytoskeleton require precise regulation of both the initiation of actin polymerization and the organization of the resulting filaments. The actin-related protein-2/3 (ARP2/3) complex is a central player in this regulation. A decade of study has begun to shed light on the molecular mechanisms by which this powerful machine controls the polymerization, organization and recycling of actin-filament networks, both in vitro and in the living cell.",

author = "Goley, \{Erin D.\} and Welch, \{Matthew D.\}",

note = "Funding Information: The precise role of ARP2/3-mediated actin polymerization in endocytosis is not yet clear. Actin polymerization might assist in invaginating the membrane, pinching off vesicles, and/or driving vesicles away from the plasma membrane121. The possibility that actin polymerization drives vesicles away from the plasma membrane is supported by the observations that endosomes, phagosomes, macropinosomes and lysosomes can rocket through the cytoplasm or through cell-free extracts by the polymerization of a closely associated comet tail of actin filaments122–125. Rocketing motility of endosomes involves the activity of the NPFs WASP or N-WASP, which localize to the surface of motile vesicles124 and are functionally important for actin assembly122,126.",

year = "2006",

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doi = "10.1038/nrm2026",

language = "English (US)",

volume = "7",

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N1 - Funding Information: The precise role of ARP2/3-mediated actin polymerization in endocytosis is not yet clear. Actin polymerization might assist in invaginating the membrane, pinching off vesicles, and/or driving vesicles away from the plasma membrane121. The possibility that actin polymerization drives vesicles away from the plasma membrane is supported by the observations that endosomes, phagosomes, macropinosomes and lysosomes can rocket through the cytoplasm or through cell-free extracts by the polymerization of a closely associated comet tail of actin filaments122–125. Rocketing motility of endosomes involves the activity of the NPFs WASP or N-WASP, which localize to the surface of motile vesicles124 and are functionally important for actin assembly122,126.

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N2 - The cellular functions of the actin cytoskeleton require precise regulation of both the initiation of actin polymerization and the organization of the resulting filaments. The actin-related protein-2/3 (ARP2/3) complex is a central player in this regulation. A decade of study has begun to shed light on the molecular mechanisms by which this powerful machine controls the polymerization, organization and recycling of actin-filament networks, both in vitro and in the living cell.

AB - The cellular functions of the actin cytoskeleton require precise regulation of both the initiation of actin polymerization and the organization of the resulting filaments. The actin-related protein-2/3 (ARP2/3) complex is a central player in this regulation. A decade of study has begun to shed light on the molecular mechanisms by which this powerful machine controls the polymerization, organization and recycling of actin-filament networks, both in vitro and in the living cell.

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U2 - 10.1038/nrm2026

DO - 10.1038/nrm2026

M3 - Review article

C2 - 16990851

AN - SCOPUS:33749037156

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EP - 726

JO - Nature Reviews Molecular Cell Biology

JF - Nature Reviews Molecular Cell Biology

IS - 10

ER -

The ARP2/3 complex: An actin nucleator comes of age

Abstract

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