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Titolo:
Activation of p38 mitogen-activated protein kinase by PYK2/related adhesion focal tyrosine kinase-dependent mechanism
Autore:
Pandey, P; Avraham, S; Kumar, S; Nakazawa, A; Place, A; Ghanem, L; Rana, A; Kumar, V; Majumder, PK; Avraham, H; Davis, RJ; Kharbanda, S;
Indirizzi:
Harvard02115, Sch Med, Dana Farber Canc Inst, Dept Adult Oncol, Boston, MAHarvard Univ Boston MA USA 02115 Canc Inst, Dept Adult Oncol, Boston, MA Harvard15nst Med, Deaconess Med Ctr, Div Expt Med & Hematol, Boston, MA 021 Harvard Inst Med Boston MA USA 02115 v Expt Med & Hematol, Boston, MA 021 Massachusetts Gen Hosp, Dept Mol Biol, Diabet Res Lab, Boston, MA 02114 USA Massachusetts Gen Hosp Boston MA USA 02114 Res Lab, Boston, MA 02114 USA Univt,Programsetts, Sch Med, Dept Biochem & Mol Biol, Howard Hughes Med Ins Univ Massachusetts Worcester MA USA 01605 Mol Biol, Howard Hughes Med Ins
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 15, volume: 274, anno: 1999,
pagine: 10140 - 10144
SICI:
0021-9258(19990409)274:15<10140:AOPMPK>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
SIGNAL-TRANSDUCTION PATHWAY; N-TERMINAL KINASE; C-JUN; MAP KINASE; IONIZING-RADIATION; STRESS-RESPONSE; GENE-EXPRESSION; ABL; PHOSPHORYLATION; CALCIUM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Kharbanda, S Harvardt,niv, Sch Med, Dana Farber Canc Inst, Dept Adult Oncol, 44 Binney S Harvard Univ 44 Binney St Boston MA USA 02115 ol, 44 Binney S
Citazione:
P. Pandey et al., "Activation of p38 mitogen-activated protein kinase by PYK2/related adhesion focal tyrosine kinase-dependent mechanism", J BIOL CHEM, 274(15), 1999, pp. 10140-10144

Abstract

The stress-activated p38 mitogen-activated protein kinase (p38 MAPK), a member of the subgroup of mammalian kinases, appears to play an important role in regulating inflammatory responses, including cytokine secretion and apoptosis, The upstream mediators that link extracellular signals with the p38 MAPK signaling pathway are currently unknown. Here we demonstrate that pp125 focal adhesion kinase-related tyrosine kinase RAFTK (also known as PYK2, CADTK) is activated specifically by methylmethane sulfonate (MMS) and hyperosmolarity but not by ultraviolet radiation, ionizing radiation, or cis-platinum. Overexpression of RAFTK leads to the activation of p38 MAPK, Furthermore, overexpression of a dominant-negative mutant of RAFTK (RAFTK K-M) inhibits MMS-induced p38 MAPK activation. MKK3 and MKK6 are known potential constituents of p38 MAPK signaling pathway, whereas SEK1 and MEK1 are upstream activators of SAPK/JNK and ERK pathways, respectively. We observe that the dominant-negative mutant of MKK3 but not of MKK6, SEK1, or MEK1 inhibits RAFTK-induced p38 MAPK activity. Furthermore, the results demonstrate that treatment of cells with 1,2-bis(2-aminophenoxy)ethane-N,N,N'.N'-tetraacetic acid, tetra(acetoxymethyl)-ester, a membrane-permeable calcium chelator,inhibits MMS-induced activation of RAFTK and p38 MAPK. Taken together, these findings indicate that RAFTK represents a stress-sensitive mediator of the p38 MAPK signaling pathway in response to certain cytotoxic agents.

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Documento generato il 08/07/20 alle ore 08:11:18