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Titolo:
CHARACTERIZATION OF RAFTK, A NOVEL FOCAL ADHESION KINASE, AND ITS INTEGRIN-DEPENDENT PHOSPHORYLATION AND ACTIVATION IN MEGAKARYOCYTES
Autore:
LI JZ; AVRAHAM H; ROGERS RA; RAJA S; AVRAHAM S;
Indirizzi:
HARVARD UNIV,SCH MED,DEACONESS HOSP,DEPT MED,DIV HEMATOL ONCOL,1 DEACONESS RD BOSTON MA 02215 HARVARD UNIV,SCH MED,DEACONESS HOSP,DEPT MED,DIV HEMATOL ONCOL BOSTONMA 02215 HARVARD UNIV,SCH PUBL HLTH,BIOMED IMAGING LAB BOSTON MA 02115
Titolo Testata:
Blood
fascicolo: 2, volume: 88, anno: 1996,
pagine: 417 - 428
SICI:
0006-4971(1996)88:2<417:CORANF>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
TYROSINE PHOSPHORYLATION; CELL-ADHESION; EXTRACELLULAR-MATRIX; CYTOSKELETON; STIMULATION; PP125(FAK); MOLECULES; BOMBESIN; LINE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
J.Z. Li et al., "CHARACTERIZATION OF RAFTK, A NOVEL FOCAL ADHESION KINASE, AND ITS INTEGRIN-DEPENDENT PHOSPHORYLATION AND ACTIVATION IN MEGAKARYOCYTES", Blood, 88(2), 1996, pp. 417-428

Abstract

We have recently isolated a cDNA encoding a novel human intracellulartyrosine kinase, termed RAFTK (for a related adhesion focal tyrosine kinase). The RAFTK cDNA, which encodes a polypeptide of 1,009 amino acids, shares 65% homology to the focal adhesion kinase (FAK), includingseveral consensus motifs. In this report, we describe the biochemicalcharacterization and functional analysis of the RAFTK protein. Coexpression of RAFTK and FAK proteins in megakaryocytic cells and blood platelets was observed. Using a specific antibody to RAFTK and the monoclonal antibody 2A7 to FAK, FAK and RAFTK could be distinguished antigenically. RAFTK had intrinsic tyrosine kinase and autokinase activities. It was phosphorylated on tyrosine in growing cultures of COS cells transfected with the pCDNAIII/flag-RAFTK expression vector containing the RAFTK cDNA ligated with the 8 amino acid flag peptide sequence. Similar to FAK, dephosphorylation of RAFTK was observed when adherent transfected COS cells were detached. Phosphorylation was regained upon replating of these cells on the fibronectin-coated dishes. Analysis of tyrosine-phosphorylated RAFTK from adherent transfected COS cells showedthat the Src homology 2 (SH2) domains of the Src and Fyn protein kinases as well as the Grb2 adaptor protein were able to specifically associate with RAFTK. Tyrosine phosphorylation of endogenous RAFTK was observed upon fibronectin-induced activation of human megakaryocytic cells. Furthermore, colocalization of RAFTK protein with vinculin, a focaladhesion protein, was observed by confocal microscopy in focal adhesion-like structures in adherent CMK cells and in transfected pCDNAIII/flag-RAFTK COS cells upon fibronectin activation. These data suggest that RAFTK is a novel member of the FAK family, that it localizes to focal adhesion-like structures in CMK megakaryocytic cells, that it participates in integrin-mediated signaling pathways in megakaryocytes, andthat it is able to associate with the tyrosine kinases Src and Fyn aswell as the adaptor protein Grb2 via SH2-phosphotyrosine interactions. (C) 1996 by The American Society of Hematology.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 07:35:07