Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
The Trio guanine nucleotide exchange factor is a RhoA target - Binding of RhoA to the Trio immunoglobulin-like domain
Autore:
Medley, QG; Serra-Pages, C; Iannotti, E; Seipel, K; Tang, M; OBrien, SP; Streuli, M;
Indirizzi:
Dana Farber Canc Inst, Dept Canc Immunol & AIDS, Boston, MA 02115 USA DanaFarber Canc Inst Boston MA USA 02115 ol & AIDS, Boston, MA 02115 USA Harvard Univ, Sch Med, Dept Pathol, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 h Med, Dept Pathol, Boston, MA 02115 USA Harvard Univ, Sch Med, Dept Med, Boston, MA 02115 USA Harvard Univ BostonMA USA 02115 Sch Med, Dept Med, Boston, MA 02115 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 46, volume: 275, anno: 2000,
pagine: 36116 - 36123
SICI:
0021-9258(20001117)275:46<36116:TTGNEF>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE-PHOSPHATASE; LIGHT-CHAIN KINASE; CELL-SHAPE CHANGES; FAMILY G-PROTEINS; ACTIN CYTOSKELETON; SIGNALING PATHWAYS; C-ELEGANS; GTPASES; VAV; ACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Streuli, M Dana Farber Canc Inst, Dept Canc Immunol & AIDS, 44 Binney St, Boston, MA 02115 USA Dana Farber Canc Inst 44 Binney St Boston MA USA 021152115 USA
Citazione:
Q.G. Medley et al., "The Trio guanine nucleotide exchange factor is a RhoA target - Binding of RhoA to the Trio immunoglobulin-like domain", J BIOL CHEM, 275(46), 2000, pp. 36116-36123

Abstract

Trio isa complex protein containing two guanine nucleotide exchange factordomains each with associated pleckstrin homology domains, a serine/threonine kinase domain, two SH3 domains, an immunoglobulin-like domain, and spectrin-like repeats. Trio was originally identified as a LAR tyrosine phosphatase-binding protein and is involved in actin remodeling, cell migration, and cell growth. Herein we provide evidence that Trio not only activates RhoAbut is also a RhoA target. The RhoA-binding site was mapped to the Trio immunoglobulin-like domain. RhoA isoprenylation is necessary for the RhoA-Trio interaction, because mutation of the RhoA carboxyl-terminal cysteine residue blocked binding, The:existence of an intramolecular functional link between RhoA activation and RhoA binding is suggested by the finding that Trioexchange activity enhanced RhoA binding to Trio. Furthermore, immunofluorescence studies of HeLa cells showed that although ectopically:expressed Trio was evenly distributed within the cell, co-expression of Trio with RhoA resulted in relocalization of Trio into punctate structures. Relocalization was not observed with Trio constructs lacking the immunoglobulin-like domain, indicating that RhoA acts to regulate,Trio localization via binding to the immunoglobulin-like domain. We propose that Trio-mediated RhoA: activation and subsequent RhoA-mediated relocalization of Trio functions to modulate and coordinate Trio signaling.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/21 alle ore 03:39:55