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Titolo:
THE RELATED ADHESION FOCAL TYROSINE KINASE IS TYROSINE-PHOSPHORYLATEDAFTER BETA-1-INTEGRIN STIMULATION IN B-CELLS AND BINDS TO P130(CAS)
Autore:
ASTIER A; AVRAHAM H; MANIE SN; GROOPMAN J; CANTY T; AVRAHAM S; FREEDMAN AS;
Indirizzi:
HARVARD UNIV,SCH MED,DANA FARBER CANC INST,DIV HEMATOL MALIGNANCIES,44 BINNEY ST BOSTON MA 02115 HARVARD UNIV,SCH MED,DANA FARBER CANC INST,DIV HEMATOL MALIGNANCIES BOSTON MA 02115 HARVARD UNIV,DEACONESS HOSP,SCH MED,DIV HEMATOL & ONCOL BOSTON MA 02115
Titolo Testata:
The Journal of biological chemistry
fascicolo: 1, volume: 272, anno: 1997,
pagine: 228 - 232
SICI:
0021-9258(1997)272:1<228:TRAFTK>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
T-LYMPHOBLASTIC CELLS; PROTEIN; PP125(FAK); FIBRONECTIN; ACTIVATION; INTEGRINS; SRC; ALPHA-4-BETA-1; ALPHA-5-BETA-1; ASSOCIATION;
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 IS TYROSINE-PHOSPHORYLATEDAFTER BETA-1-INTEGRIN STIMULATION IN B-CELLS AND BINDS TO P130(CAS)", The Journal of biological chemistry, 272(1), 1997, pp. 228-232

Abstract

Integrin ligation initiates intracellular signaling events, among which are the activation of protein tyrosine kinases. The related adhesion focal tyrosine kinase (RAFTK), also known as PYK2 and CAK beta, is atyrosine kinase that is homologous to the focal adhesion kinase (FAK)p125(FAK). The structure of RAFTK is similar to p125(FAK) in that it lacks a transmembrane region, does not contain Src homology 2 or 3 domains, and has a proline rich region in its C terminus. Here we report that RAFTK is a target for beta 1-integrin-mediated tyrosine phosphorylation in both transformed and normal human B cells. Ligation of the Bcell antigen receptor also induced tyrosine phosphorylation of RAFTK. Phosphorylation of RAFTK following integrin- or B cell antigen receptor-mediated stimulation was decreased by prior treatment of cells withcytochalasin B, indicating that this process was at least partially cytoskeleton-dependent. One of the tyrosine-phosphorylated substrates after integrin stimulation in fibroblasts is p130(cas), which can associate with p125(FAK). RAFTK also interacted constitutively with p130(cas) in B cells, since p130(cas) was detected in RAFTK immunoprecipitates. Although the function of RAFTK remains unknown, these data suggest that RAFTK may have a significant function in integrin-mediated signaling pathways in B cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 22:29:05