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Titolo:
Increased filamin binding to beta-integrin cytoplasmic domains inhibits cell migration
Autore:
Calderwood, DA; Huttenlocher, A; Kiosses, WB; Rose, DM; Woodside, DG; Schwartz, MA; Ginsberg, MH;
Indirizzi:
Scripps Clin & Res Inst, Dept Vasc Biol, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 iol, La Jolla, CA 92037 USA Univ Wisconsin, Dept Pediat, Madison, WI 53706 USA Univ Wisconsin MadisonWI USA 53706 n, Dept Pediat, Madison, WI 53706 USA Univ Wisconsin, Dept Pharmacol, Madison, WI 53706 USA Univ Wisconsin Madison WI USA 53706 Dept Pharmacol, Madison, WI 53706 USA Scripps Clin & Res Inst, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 nst, La Jolla, CA 92037 USA
Titolo Testata:
NATURE CELL BIOLOGY
fascicolo: 12, volume: 3, anno: 2001,
pagine: 1060 - 1068
SICI:
1465-7392(200112)3:12<1060:IFBTBC>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALPHA-ACTININ; TRANSMEMBRANE LINKAGE; FIBRONECTIN MATRIX; TARGETS FILAMIN; FOCAL ADHESIONS; PROTEIN; ACTIVATION; TALIN; IDENTIFICATION; GLYCOPROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Ginsberg, MH Scripps Clin & Res Inst, Dept Vasc Biol, 10550 N Torrey PinesRd, La Jolla, CA 92037 USA Scripps Clin & Res Inst 10550 N Torrey Pines RdLa Jolla CA USA 92037
Citazione:
D.A. Calderwood et al., "Increased filamin binding to beta-integrin cytoplasmic domains inhibits cell migration", NAT CELL BI, 3(12), 2001, pp. 1060-1068

Abstract

Multicellular animal development depends on integrins. These adhesion receptors link to the actin cytoskeleton, transmitting biochemical signals and force during cell migration and interactions with the extracellular matrix. Many integrin-cytoskeleton connections are formed by filamins and talin. The beta (7) integrin tail binds strongly to filamin and supports less migration, fibronectin matrix assembly and focal adhesion formation than either the beta (1D) tail, which binds strongly to talin, or the beta (1A) tail, which binds modestly to both filamin and talin. To probe the role of filaminbinding, we mapped the filamin-binding site of integrin tails and identified amino acid substitutions that led to selective loss of filamin binding to the beta (7) tail and gain of filamin binding to the beta (1A) tail. These changes affected cell migration and membrane protrusions but not fibronectin matrix assembly or focal adhesion formation. Thus, tight filamin binding restricts integrin-dependent cell migration by inhibiting transient membrane protrusion and cell polarization.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/04/20 alle ore 22:37:36