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Titolo:
Differential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25Mm
Autore:
Giglione, C; Gonfloni, S; Parmeggiani, A;
Indirizzi:
Ecole Polytech, Grp Biophys, Equipe 2, Palaiseau, France Ecole Polytech Palaiseau France rp Biophys, Equipe 2, Palaiseau, France European Mol Biol Lab, Heidelberg, Germany European Mol Biol Lab Heidelberg Germany Biol Lab, Heidelberg, Germany
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 11, volume: 268, anno: 2001,
pagine: 3275 - 3283
SICI:
0014-2956(200106)268:11<3275:DAOPAL>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTPASE-ACTIVATING PROTEIN; BETA-GAMMA-SUBUNITS; TYROSINE KINASE; NUCLEOTIDE EXCHANGE; DEPENDENT ACTIVATION; CATALYTIC DOMAIN; V-SRC; PHOSPHATIDYLINOSITOL 3-KINASE; BINDING-PROTEIN; RHO-FAMILY;
Keywords:
RasGAP; RasGEF; CDC25Mm; Src; Lck;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Giglione, C CNRS, Inst Sci Vegetal, Unite Propre Rech 2355, Bat 23,Ave Terrasse, F-91198 Gif Sur Yvette, France CNRS Bat 23,Ave Terrasse Gif Sur Yvette France F-91198 France
Citazione:
C. Giglione et al., "Differential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25Mm", EUR J BIOCH, 268(11), 2001, pp. 3275-3283

Abstract

It is known that the human Ras GTPase activating protein (GAP) p120-GAP can be phosphorylated by different members of the Src kinase family and recently phosphorylation of the GDP/GTP exchange factor (GEF) CDC25Mm/ GRF1 by proteins of the Src kinase family has been revealed in vivo [Kiyono, M., Kaziro, Y. & Satoh, T. (2000) J. Biol. Chem. 275, 5441-5446]. As it still remains unclear how these phosphorylations can influence the Ras pathway we have analyzed the ability of p60c-Src and Lck to phosphorylate these two Ras regulators and have compared the activity of the phosphorylated and unphosphorylated forms. Both kinases were found to phosphorylate full-length or truncated forms of GAP and GEE The use of the catalytic domain of p60c-Src showed that its SH3/SH2 domains are not required for the interaction and the phosphorylation of both regulators. Remarkably, the phosphorylations by the two kinases were accompanied by different functional effects. The phosphorylation of p120-GAP by p60c-Src inhibited its ability to stimulate the Ha-Ras-GTPase activity, whereas phosphorylation by Lck did not display any effect. A different picture became evident with CDC25Mm; phosphorylation by Lck increased its capacity to stimulate the GDP/GTP exchange on Ha-Ras, whereasits phosphorylation by p60c-Src was ineffective. Our results suggest that phosphorylation by p60c-Src and Lck is a selective process that can modulate the activity of p120-GAP and CDC25Mm towards Ras proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 05:57:57