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Titolo:
Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1
Autore:
Kim, AH; Khursigara, G; Sun, X; Franke, TF; Chao, MV;
Indirizzi:
NYU, Sch Med, Skirball Inst Biomol Med, Mol Neurobiol Program, New York, NY 10016 USA NYU New York NY USA 10016 , Mol Neurobiol Program, New York, NY 10016 USA Columbia Univ, Dept Pharmacol, New York, NY 10032 USA Columbia Univ New York NY USA 10032 ept Pharmacol, New York, NY 10032 USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 3, volume: 21, anno: 2001,
pagine: 893 - 901
SICI:
0270-7306(200102)21:3<893:APANRA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIVATED PROTEIN-KINASE; GLYCOGEN-SYNTHASE KINASE-3; PROMOTES CELL-SURVIVAL; N-TERMINAL KINASE; TRANSCRIPTION FACTOR; PHOSPHATIDYLINOSITOL 3-KINASE; TRANSDUCTION PATHWAY; KAPPA-B; ASK1; DEATH;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Chao, MV NYU, Med Ctr, Skirball Inst, 540 1st Ave,Rm 5-15, New York, NY 10016 USA NYU 540 1st Ave,Rm 5-15 New York NY USA 10016 York, NY 10016 USA
Citazione:
A.H. Kim et al., "Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1", MOL CELL B, 21(3), 2001, pp. 893-901

Abstract

The Akt family of serine/threonine-directed kinases promotes cellular survival in part by phosphorylating and inhibiting death-inducing proteins. Here we describe a novel functional interaction between Akt and apoptosis signal-regulating kinase 1 (ASK1), a mitogen-activated protein kinase kinase kinase. Akt decreased ASK1 kinase activity stimulated by both oxidative stress and overexpression in 293 cells by phosphorylating a consensus Akt site at serine 83 of ASK1. Activation of the phosphoinositide 3-kinase (PI3-K)/Akt pathway also inhibited the serum deprivation-induced activity of endogenous ASK1 in L929 cells. An association between Akt and ASK1 was detected in cells by coimmunoprecipitation. Phosphorylation by Akt inhibited ASK1-mediated c-Jun N-terminal kinase and activating transcription factor 2 activities in intact cells. Finally, activation of the PI3-K/Akt pathway reduced apoptosis induced by ASK1 in a manner dependent on phosphorylation of serine 83 of ASK1. These results provide the first direct link between Akt and the family of stress-activated kinases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 02:11:46