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Titolo:
Characterization of RasGRP2, a plasma membrane-targeted, dual specificity Ras/Rap exchange factor
Autore:
Clyde-Smith, J; Silins, G; Gartside, M; Grimmond, S; Etheridge, M; Apolloni, A; Hayward, N; Hancock, JF;
Indirizzi:
Univ Queensland, Sch Med, Dept Pathol, Queensland Canc Fund,Lab Expt Oncol, Brisbane, Qld 4006, Australia Univ Queensland Brisbane Qld Australia 4006 Brisbane, Qld 4006, Australia Queensland Inst Med Res, Bancroft Ctr, Queensland Canc Fund, Res Unit, Brisbane, Qld 4006, Australia Queensland Inst Med Res Brisbane Qld Australia 4006 , Qld 4006, Australia
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 41, volume: 275, anno: 2000,
pagine: 32260 - 32267
SICI:
0021-9258(20001013)275:41<32260:CORAPM>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
GUANINE-NUCLEOTIDE EXCHANGE; RAS SIGNALING PATHWAY; BINDING DOMAIN; FACTOR SOS; ACTIVATION; PROTEIN; GRB2; RECEPTOR; SHC; COMPLEXES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Hancock, JF Univ Queensland, Sch Med, Dept Pathol, Queensland Canc Fund,Lab Expt Oncol, Herston Rd, Brisbane, Qld 4006, Australia Univ Queensland Herston Rd Brisbane Qld Australia 4006 stralia
Citazione:
J. Clyde-Smith et al., "Characterization of RasGRP2, a plasma membrane-targeted, dual specificity Ras/Rap exchange factor", J BIOL CHEM, 275(41), 2000, pp. 32260-32267

Abstract

Ras proteins operate as molecular switches in signal transduction pathwaysdownstream of tyrosine kinases and G-protein-coupled receptors. Ras is switched from the inactive GDP-bound state to the active GTP-bound state by guanine nucleotide exchange factors (GEFs), We report here the cloning and characterization of RasGRP2, a longer alternatively spliced form of the recently cloned RapGEF, CalDAG-GEFI. A unique feature of RasGRP2 is that it is targeted to the plasma membrane by a combination of N-terminal myristoylation and palmitoylation. In vivo, RasGRP2 selectively catalyzes nucleotide exchange on N- and Ki-Ras, but not Ha-Pas. RasGRP2 also catalyzes nucleotide exchange on Rap1, but this RapGEF activity is less potent than that associated with CalDAG-GEFI. The nucleotide exchange activity of RasGRP2 toward N-Ras is stimulated by diacylglycerol and inhibited by calcium. The effects ofdiacylglycerol and calcium are additive but are not accompanied by any detectable change in the subcellular localization of RasGRP2. In contrast, CalDAG-GEFI is localized predominantly to the cytosol and lacks Pas exchange activity in vivo. However, prolonged exposure to phorbol esters, or growth in serum, results in localization of CalDAG-GEFI to the cell membrane and restoration of Pas exchange activity. Expression of RasGRP2 or CalDAG-GEFI inNIH3T3 cells transfected with wild type N-Ras results in an accelerated growth rate but not morphologic transformation. Thus, under appropriate growth conditions, CalDAG-GEFI and RasGRP2 are dual specificity Ras and Rap exchange factors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 07:03:45