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

Biochemistry, Genetics and Molecular Biology(all)
Agricultural and Biological Sciences(all)

Access to Document

10.1016/S0960-9822(03)00160-X

Cite this

@article{23ca03f229bb4e75938644355126828f,

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",

year = "2003",

month = mar,

day = "18",

doi = "10.1016/S0960-9822(03)00160-X",

language = "English (US)",

volume = "13",

pages = "R236--R238",

journal = "Current Biology",

issn = "0960-9822",

publisher = "Cell Press",

number = "6",

}

TY - JOUR

T1 - Lamellipodia protrusion

T2 - Moving interactions of vinculin and Arp2/3

AU - Craig, Susan W.

AU - Chen, Hui

PY - 2003/3/18

Y1 - 2003/3/18

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=0037452873&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037452873&partnerID=8YFLogxK

U2 - 10.1016/S0960-9822(03)00160-X

DO - 10.1016/S0960-9822(03)00160-X

M3 - Short survey

C2 - 12646151

AN - SCOPUS:0037452873

SN - 0960-9822

VL - 13

SP - R236-R238

JO - Current Biology

JF - Current Biology

IS - 6

ER -

Lamellipodia protrusion: Moving interactions of vinculin and Arp2/3

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this