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Titolo:
THE RELATED ADHESION FOCAL TYROSINE KINASE DIFFERENTIALLY PHOSPHORYLATES P130(CAS) AND THE CAS-LIKE PROTEIN, P105(HEF1)
Autore:
ASTIER A; MANIE SN; AVRAHAM H; HIRAI H; LAW SF; ZHANG YH; GOLEMIS EA; FU YG; DRUKER BJ; HAGHAYEGHI N; FREEDMAN AS; AVRAHAM S;
Indirizzi:
DANA FARBER CANC INST,DIV HEMATOL MALIGNANCIES,44 BINNEY ST BOSTON MA02115 DANA FARBER CANC INST,DIV HEMATOL MALIGNANCIES BOSTON MA 02115 HARVARD UNIV,SCH MED,DEPT MED BOSTON MA 02115 BETH ISRAEL DEACONESS MED CTR,DIV EXPT MED & HEMATOL ONCOL RES BOSTONMA 02115 UNIV TOKYO,DEPT INTERNAL MED 3 TOKYO 113 JAPAN FOX CHASE CANC CTR,INST CANC RES PHILADELPHIA PA 19111 OREGON HLTH SCI UNIV,DIV HEMATOL & MED ONCOL PORTLAND OR 97201
Titolo Testata:
The Journal of biological chemistry
fascicolo: 32, volume: 272, anno: 1997,
pagine: 19719 - 19724
SICI:
0021-9258(1997)272:32<19719:TRAFTK>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
SRC; DOMAIN; CRK; MEGAKARYOCYTES; IDENTIFICATION; FIBRONECTIN; CELLS; C3G;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
A. Astier et al., "THE RELATED ADHESION FOCAL TYROSINE KINASE DIFFERENTIALLY PHOSPHORYLATES P130(CAS) AND THE CAS-LIKE PROTEIN, P105(HEF1)", The Journal of biological chemistry, 272(32), 1997, pp. 19719-19724

Abstract

The related adhesion focal tyrosine kinase (RAFTK) is tyrosine-phosphorylated following beta 1 integrin or B cell antigen receptor stimulation in human B cells. Two substrates that are tyrosine-phosphorylated following integrin ligation in B cells are p130(Cas) and the Cas family member human enhancer of filamentation 1 (HEF1), both of which can associate with RAFTK. In this report we observed that RAFTK was involved in the phosphorylation of these two proteins. While a catalytically active RAFTK was required for both p130(Cas) and HEF1, phosphorylationof p130(Cas), but not of HEF1, was dependent on an intact autophosphorylation site (Tyr(402)) on RAFTK. To determine if RAFTK phosphorylated p130(Cas) and HEF1 directly or through an intermediate, we assayed the ability of RAFTK and of a Tyr(402) mutant to phosphorylate purifiedHEF1 and p130(Cas) domains. RAFTK was able to phosphorylate the substrate domains of both p130(Cas) and HEF1, but only the C-terminal domain of p130(Cas). Furthermore, Tyr(402), which mediates the binding of RAFTK to c-Src kinase, was required for the phosphorylation of the C-terminal domain of p130(Cas). These data suggest that RAFTK itself is sufficient for HEF1 phosphorylation, whereas a cooperation between RAFTKand Src kinases is required for the complete phosphorylation of p130(Cas).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 22:13:20