Lamellipodia protrusion: Moving interactions of vinculin and Arp2/3

Susan W. Craig; Hui Chen

doi:10.1016/S0960-9822(03)00160-X

Lamellipodia protrusion: Moving interactions of vinculin and Arp2/3

Susan W. Craig, Hui Chen

School of Medicine

Research output: Contribution to journal › Short survey › peer-review

17 Scopus citations

Abstract

A direct, transient interaction between vinculin and Arp2/3 is required to promote receptor-stimulated lamellipodial extension and cell spreading. Vinculin selectively recruits Arp2/3 to the leading edge of the lamellipodium, where it may couple the actin polymerization machinery to adhesion complexes to promote membrane protrusion over ruffling.

Original language	English (US)
Pages (from-to)	R236-R238
Journal	Current Biology
Volume	13
Issue number	6
DOIs	https://doi.org/10.1016/S0960-9822(03)00160-X
State	Published - Mar 18 2003

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology
General Agricultural and Biological Sciences

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10.1016/S0960-9822(03)00160-X

Cite this

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title = "Lamellipodia protrusion: Moving interactions of vinculin and Arp2/3",

abstract = "A direct, transient interaction between vinculin and Arp2/3 is required to promote receptor-stimulated lamellipodial extension and cell spreading. Vinculin selectively recruits Arp2/3 to the leading edge of the lamellipodium, where it may couple the actin polymerization machinery to adhesion complexes to promote membrane protrusion over ruffling.",

author = "Craig, {Susan W.} and Hui Chen",

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AU - Chen, Hui

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AB - A direct, transient interaction between vinculin and Arp2/3 is required to promote receptor-stimulated lamellipodial extension and cell spreading. Vinculin selectively recruits Arp2/3 to the leading edge of the lamellipodium, where it may couple the actin polymerization machinery to adhesion complexes to promote membrane protrusion over ruffling.

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Lamellipodia protrusion: Moving interactions of vinculin and Arp2/3

Abstract

ASJC Scopus subject areas

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