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Titolo:
JUXTAMEMBRANE TYROSINE RESIDUES COUPLE THE EPH FAMILY RECEPTOR EPHB2 NUK TO SPECIFIC SH2 DOMAIN PROTEINS IN NEURONAL CELLS/
Autore:
HOLLAND SJ; GALE NW; GISH GD; ROTH RA; ZHOU SY; CANTLEY LC; HENKEMEYER M; YANCOPOULOS GD; PAWSON T;
Indirizzi:
MT SINAI HOSP,SAMUEL LUNENFELD RES INST,PROGRAMME MOL BIOL & CANC,600UNIV AVE TORONTO ON M5G 1X5 CANADA MT SINAI HOSP,SAMUEL LUNENFELD RES INST,PROGRAMME MOL BIOL & CANC TORONTO ON M5G 1X5 CANADA REGENERON PHARMACEUT INC TARRYTOWN NY 10804 STANFORD UNIV,SCH MED,DEPT MOL PHARMACOL STANFORD CA 94305 BETH ISRAEL HOSP,DEPT MED,DIV SIGNAL TRANSDUCT BOSTON MA 02115 UNIV TORONTO,DEPT MOL & MED GENET TORONTO ON M5G 1A8 CANADA
Titolo Testata:
EMBO journal
fascicolo: 13, volume: 16, anno: 1997,
pagine: 3877 - 3888
SICI:
0261-4189(1997)16:13<3877:JTRCTE>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTPASE-ACTIVATING PROTEIN; ACTIN STRESS FIBERS; MOLECULAR-CLONING; AXON GUIDANCE; GROWTH CONE; KINASE; LIGAND; SRC; GAP; RHO;
Keywords:
EPH FAMILY RECEPTOR; EPHRIN; NEURONAL SIGNALING; RAS GTPASE-ACTIVATING PROTEIN; TYROSINE PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
63
Recensione:
Indirizzi per estratti:
Citazione:
S.J. Holland et al., "JUXTAMEMBRANE TYROSINE RESIDUES COUPLE THE EPH FAMILY RECEPTOR EPHB2 NUK TO SPECIFIC SH2 DOMAIN PROTEINS IN NEURONAL CELLS/", EMBO journal, 16(13), 1997, pp. 3877-3888

Abstract

Eph-related receptor tyrosine kinases have been implicated in the control of axonal navigation and fasciculation. To investigate the biochemical mechanisms underlying such functions, we have expressed the EphB2 receptor (formerly Nuk/Cek5/Sek3) in neuronal NG108-15 cells, and have observed the tyrosine phosphorylation of multiple cellular proteinsupon activation of EphB2 by its ligand, ephrin-B1 (formerly Elk-L/Lerk2). The activated EphB2 receptor induced the tyrosine phosphorylationof a 62-64 kDa protein (p62(dok)), which in turn formed a complex with the Ras GTPase-activating protein (RasGAP) and SH2/SH3 domain adaptor protein Nck, RasGAP also bound through its SH2 domains to tyrosine-phosphorylated EphB2 in vitro, and complexed with activated EphB2 in vivo. We have localized an in vitro RasGAP-binding site to conserved tyrosine residues Y604 and Y610 in the juxtamembrane region of EphB2, anddemonstrated that substitution of these amino acids abolishes ephrin-B1-induced signalling events in EphB2-expressing NG108-15 cells. Thesetyrosine residues are followed by proline at the +3 position, consistent with the binding specificity of RasGAP SH2 domains determined using a degenerate phosphopeptide library. These results identify an EphB2-activated signalling cascade involving proteins that potentially playa role in axonal guidance and control of cytoskeletal architecture.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:30:49