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Titolo:
INTERACTION OF P72(SYK) WITH THE GAMMA-SUBUNITS AND BETA-SUBUNITS OF THE HIGH-AFFINITY RECEPTOR FOR IMMUNOGLOBULIN-E, IMMUNOGLOBULIN-FC-EPSILON-RI
Autore:
SHIUE L; GREEN J; GREEN OM; KARAS JL; MORGENSTERN JP; RAM MK; TAYLOR MK; ZOLLER MJ; ZYDOWSKY LD; BOLEN JB; BRUGGE JS;
Indirizzi:
ARIAD PHARMACEUT INC,26 LANDSDOWNE ST CAMBRIDGE MA 02139 ARIAD PHARMACEUT INC CAMBRIDGE MA 02139 BRISTOL MYERS SQUIBB PHARMACEUT RES INST,DEPT MOLEC BIOL PRINCETON NJ08543
Titolo Testata:
Molecular and cellular biology
fascicolo: 1, volume: 15, anno: 1995,
pagine: 272 - 281
SICI:
0270-7306(1995)15:1<272:IOPWTG>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASE; CELL ANTIGEN RECEPTOR; SOLID-PHASE SYNTHESIS; T-CELL; SIGNAL-TRANSDUCTION; SH2 DOMAINS; ZETA-CHAIN; PHOSPHATIDYLINOSITOL 3-KINASE; PHOSPHOTYROSYL PEPTIDE; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
L. Shiue et al., "INTERACTION OF P72(SYK) WITH THE GAMMA-SUBUNITS AND BETA-SUBUNITS OF THE HIGH-AFFINITY RECEPTOR FOR IMMUNOGLOBULIN-E, IMMUNOGLOBULIN-FC-EPSILON-RI", Molecular and cellular biology, 15(1), 1995, pp. 272-281

Abstract

Activation of protein tyrosine kinases is one of the initial events following aggregation of the high-affinity receptor for immunoglobulin E (Fc epsilon RI) on RBL-2H3 cells, a model mast cell line. The protein tyrosine kinase p72(syk) (Syk), which contains two Src homology 2 (SH2) domains, is activated and associates with phosphorylated Fc epsilon RI subunits after receptor aggregation. In this report, we used Syk SH2 domains, expressed in tandem or individually, as fusion proteins to identify Syk-binding proteins in RBL-2H3 lysates. We show that the tandem Syk SH2 domains selectively associate with tyrosine-phosphorylated forms of the gamma and beta subunits of Fc epsilon RI. The isolatedcarboxy-proximal SH2 domain exhibited a significantly higher affinityfor the Fc epsilon RI subunits than did the amino-proximal domain. When in tandem, the Syk SH2 domains showed enhanced binding to phosphorylated gamma and beta subunits. The conserved tyrosine-based activationmotifs contained in the cytoplasmic domains of the gamma and beta subunits, characterized by two YXXL/I sequences in tandem, represent potential high-affinity binding sites for the dual SH2 domains of Syk. Peptide competition studies indicated that Syk exhibits a higher affinityfor the phosphorylated tyrosine activation motif of the gamma subunitthan for that of the beta subunit. In addition, we show that Syk is the major protein in RBL-2H3 cells that is affinity isolated with phosphorylated peptides corresponding to the phosphorylated gamma subunit motif. These data suggest that Syk associates with the gamma subunit ofthe high-affinity receptor for immunoglobulin E through an interaction between the tandem SH2 domains of Syk and the phosphorylated tyrosine activation motif of the gamma subunit and that Syk may be the major signaling protein that binds to Fc epsilon RI tyrosine activation motifs in RBL-2H3 cells.

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Documento generato il 13/07/20 alle ore 09:38:24