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Titolo:
Intersectin can regulate the Ras/MAP kinase pathway independent of its role in endocytosis
Autore:
Tong, XK; Hussain, NK; Adams, AG; OBryan, JP; McPherson, PS;
Indirizzi:
McGill Univ, Montreal Neurol Inst, Dept Neurol & Neurosurg, Montreal, PQ H3A 2B4, Canada McGill Univ Montreal PQ Canada H3A 2B4 surg, Montreal, PQ H3A 2B4, Canada NIEHS, Lab Signal Transduct, Res Triangle Pk, NC 27709 USA NIEHS Res Triangle Pk NC USA 27709 ansduct, Res Triangle Pk, NC 27709 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 38, volume: 275, anno: 2000,
pagine: 29894 - 29899
SICI:
0021-9258(20000922)275:38<29894:ICRTRK>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIVATED PROTEIN-KINASE; EPIDERMAL GROWTH-FACTOR; NUCLEOTIDE EXCHANGE FACTOR; CLATHRIN-MEDIATED ENDOCYTOSIS; RECEPTOR INTERNALIZATION; SIGNAL-TRANSDUCTION; PHENYLARSINE OXIDE; ADAPTER PROTEIN; EPS15 HOMOLOGY; BETA-ARRESTIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: McPherson, PS McGill Univ, Montreal Neurol Inst, Dept Neurol & Neurosurg, 3801 Univ St, Montreal, PQ H3A 2B4, Canada McGill Univ 3801 Univ St Montreal PQ Canada H3A 2B4 , Canada
Citazione:
X.K. Tong et al., "Intersectin can regulate the Ras/MAP kinase pathway independent of its role in endocytosis", J BIOL CHEM, 275(38), 2000, pp. 29894-29899

Abstract

We previously identified intersectin, a multiple EH and SH3 domain-containing protein, as a component of the endocytic machinery. Overexpression of the SH3 domains of intersectin blocks transferrin receptor endocytosis, possibly by disrupting targeting of accessory proteins of clathrin-coated pit formation. More recently, we identified mammalian Sos, a guanine-nucleotide exchange factor for Pas, as an intersectin SH3 domain-binding partner. We now demonstrate that overexpression of intersectin's SH3 domains blocks activation of Ras and MAP kinase in various cell lines. Several studies suggestthat activation of MAP kinase downstream of multiple receptor types is dependent on endocytosis. Thus, the dominant-negative effect of the SH3 domains on Ras/MAP kinase activation may be indirectly mediated through a block in endocytosis. Consistent with this idea, incubating cells at 4 degrees C or with phenylarsine oxide, treatments previously established to inhibit EGFreceptor endocytosis, blocks EGF-dependent activation of MAP kinase. However, under these conditions, Pas activity is unaffected and overexpression of the SH3 domains of intersectin is still able to block Pas activation. Thus, intersectin SH3 domain overexpression can effect EGF-mediated MAP kinaseactivation directly through a block in Pas, consistent with a functional role for intersectin in Ras activation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 08:34:30