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Titolo:
CATALYTIC SPECIFICITY OF PROTEIN-TYROSINE KINASES IS CRITICAL FOR SELECTIVE SIGNALING
Autore:
SONGYANG Z; CARRAWAY KL; ECK MJ; HARRISON SC; FELDMAN RA; MOHAMMADI M; SCHLESSINGER J; HUBBARD SR; SMITH DP; ENG C; LORENZO MJ; PONDER BAJ; MAYER BJ; CANTLEY LC;
Indirizzi:
BETH ISRAEL HOSP,DEPT MED,DIV SIGNAL TRANSDUCT BOSTON MA 02215 BETH ISRAEL HOSP,DEPT MED,DIV SIGNAL TRANSDUCT BOSTON MA 02215 HARVARD UNIV,SCH MED,DEPT CELL BIOL BOSTON MA 02215 TUFTS UNIV,SCH MED,DEPT PHYSIOL BOSTON MA 02111 CHILDRENS HOSP,HOWARD HUGHES MED INST BOSTON MA 02115 CHILDRENS HOSP,MOLEC MED LAB BOSTON MA 02115 UNIV MARYLAND,SCH MED,DEPT MICROBIOL & IMMUNOL BALTIMORE MD 21201 UNIV MARYLAND,MARYLAND BIOTECHNOL INST,CTR MED BIOTECHNOL BALTIMORE MD 21201 NYU,MED CTR,DEPT PHARMACOL NEW YORK NY 10016 COLUMBIA UNIV,DEPT BIOCHEM & MOLEC BIOPHYS NEW YORK NY 10032 UNIV CAMBRIDGE,DEPT PATHOL,CRC,HUMAN CANC GENET RES GRP CAMBRIDGE CB21QP ENGLAND HARVARD UNIV,SCH MED,DANA FARBER CANC INST,DEPT MED BOSTON MA 02115 HARVARD UNIV,SCH MED,DEPT MICROBIOL & MOLEC GENET BOSTON MA 02115
Titolo Testata:
Nature
fascicolo: 6514, volume: 373, anno: 1995,
pagine: 536 - 539
SICI:
0028-0836(1995)373:6514<536:CSOPKI>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
SUBSTRATE-SPECIFICITY; PHOSPHORYLATION; DOMAINS; INVITRO; ANTIGEN; SITES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
Z. Songyang et al., "CATALYTIC SPECIFICITY OF PROTEIN-TYROSINE KINASES IS CRITICAL FOR SELECTIVE SIGNALING", Nature, 373(6514), 1995, pp. 536-539

Abstract

How do distinct protein-tyrosine kinases activate specific downstreamevents? Src-homology-2 (SH2) domains on tyrosine kinases or targets of tyrosine kinases recognize phosphotyrosine in a specific sequence context and thereby provide some specificity(1-3). The role of the catalytic site of tyrosine kinases in determining target specificity has not been fully investigated. Here we use a degenerate peptide library toshow that each of nine tyrosine kinases investigated has a unique optimal peptide substrate. We find that the cytosolic tyrosine kinases preferentially phosphorylate peptides recognized by their own SH2 domains or closely related SH2 domains (group I; ref. 3), whereas receptor tyrosine kinases preferentially phosphorylate peptides recognized by subsets of group In SH2 domains(3). The importance of these findings forhuman disease is underscored by our observation that a point mutationin the RET receptor-type tyrosine kinase, which causes multiple endocrine neoplasia type 2B, results in a shift in peptide substrate specificity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 05:20:25