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Titolo:
Characterization of the tyrosine kinases RAFTK/Pyk2 and FAK in nerve growth factor-induced neuronal differentiation
Autore:
Park, SY; Avraham, H; Avraham, S;
Indirizzi:
Harvard Univ, Sch Med, Beth Israel Deaconess Med Ctr, Harvard Inst Med,DivExpt Med, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 st Med,DivExpt Med, Boston, MA 02115 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 26, volume: 275, anno: 2000,
pagine: 19768 - 19777
SICI:
0021-9258(20000630)275:26<19768:COTTKR>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
FOCAL ADHESION KINASE; PC12 CELLS; SIGNAL-TRANSDUCTION; RAPID REDISTRIBUTION; IN-VITRO; F-ACTIN; PAXILLIN; PHOSPHORYLATION; CALCIUM; IDENTIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Avraham, S Harvard Univ, Sch Med, Beth Israel Deaconess Med Ctr, Harvard Inst Med,DivExpt Med, 4 Blackfan Circle, Boston, MA 02115 USA Harvard Univ 4Blackfan Circle Boston MA USA 02115 MA 02115 USA
Citazione:
S.Y. Park et al., "Characterization of the tyrosine kinases RAFTK/Pyk2 and FAK in nerve growth factor-induced neuronal differentiation", J BIOL CHEM, 275(26), 2000, pp. 19768-19777

Abstract

The related adhesion focal tyrosine kinase (RAFTK), a member of the focal adhesion kinase (FAK) family and highly expressed in brain, is a key mediator of various extracellular signals that elevate intracellular Ca2+ concentration. We investigated RAFTK and FAK signaling upon nerve growth factor (NGF) stimulation of PC12 cells. NGF induced the tyrosine phosphorylation of RAFTK in a time- and dose-dependent manner, whereas no change in the tyrosine phosphorylation of FAK was observed Chemical inhibition showed that RAFTK phosphorylation was inhibited by blocking phospholipase Cy activity or intracellular Ca2+. Blocking of extracellular Ca2+ or phosphatidylinositol 3-kinase activity partially reduced the phosphorylation of RAFTK. In addition, disruption of actin polymerization abolished RAFTK phosphorylation, indicating that an intact actin-based cytoskeletal organization is required for RAFTK phosphorylation. The focal adhesion molecule paxillin was co-immunoprecipitated with RAFTK, and its tyrosine phosphorylation was increased in a Ca2+-dependent manner upon NGF stimulation. Confocal microscopic analysis demonstrated that RAFTK translocated from the cytoplasm to potential neuriteinitiation sites at the cell periphery, where RAFTK co-localized with paxillin and bundled actin in the early phase (within 5 min) of NGF stimulation, whereas FAK co-localized with paxillin at "point contacts," which are theprimary cell adhesion sites in neuronal cells. Significant distribution ofRAFTK was observed in the neurites and growth cones of differentiated PC12cells. Furthermore, potassium depolarization induced the tyrosine phosphorylation of both RAFTK and paxillin in an intracellular Ca2+ dependent manner in the differentiated PC12 cells. Taken together, these results demonstrate that RAFTK is involved in NGF-induced cytoskeletal organization and may play a role in neurite and growth cone function(s).

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Documento generato il 03/07/20 alle ore 22:50:20