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Titolo:
Negative regulation of the SHPTP1 protein tyrosine phosphatase by protein kinase c delta in response to DNA damage
Autore:
Yoshida, K; Kufe, D;
Indirizzi:
Harvard Univ, Sch Med, Dana Farber Canc Inst, Boston, MA 02115 USA HarvardUniv Boston MA USA 02115 a Farber Canc Inst, Boston, MA 02115 USA
Titolo Testata:
MOLECULAR PHARMACOLOGY
fascicolo: 6, volume: 60, anno: 2001,
pagine: 1431 - 1438
SICI:
0026-895X(200112)60:6<1431:NROTSP>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
MYELOID-LEUKEMIA CELLS; IONIZING-RADIATION; SH2 DOMAIN; PROTEOLYTIC ACTIVATION; CELLULAR-RESPONSE; STRESS-RESPONSE; MOTH-EATEN; 1-BETA-D-ARABINOFURANOSYLCYTOSINE; EXPRESSION; INDUCTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Kufe, D Harvard Univ, Sch Med, Dana Farber Canc Inst, 44 Binney St, Boston, MA 02115 USA Harvard Univ 44 Binney St Boston MA USA 02115 Boston, MA 02115 USA
Citazione:
K. Yoshida e D. Kufe, "Negative regulation of the SHPTP1 protein tyrosine phosphatase by protein kinase c delta in response to DNA damage", MOLEC PHARM, 60(6), 2001, pp. 1431-1438

Abstract

The SHPTP1 protein tyrosine phosphatase is activated by the c-Abl and Lyn tyrosine kinases in the cellular response to genotoxic stress. However, signaling mechanisms involved in the negative regulation of SHPTP1 are unknown. This study demonstrates that protein kinase C delta (PKC delta) associates with SHPTP1. The PKC delta catalytic domain binds directly to SHPTP1. Theresults also demonstrate that PKC delta is required, at least in part, forphosphorylation and inactivation of SHPTP1. The phosphatase activity of SHPTP1 was attenuated by coincubation with PKC delta in vitro. In addition, treatment of U-937 human myeloid leukemia cells with 1-beta -D-arabinofuranosylcytosine (ara-C) was associated with induction of the PKC delta kinase function and inhibition of SHPTP1 activity. Down-regulation of SHPTP1 by ara-C was blocked by the PKC delta inhibitor rottlerin but not by the PKC alpha and -beta inhibitor Go6976. Moreover, transient coexpression studies witha dominant-negative mutant of PKC delta demonstrate that the kinase activity of PKC delta is required for the down-regulation of SHPTP1. These findings support the functional interaction between PKC delta and SHPTP1 in the cellular response to DNA damage.

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Documento generato il 02/04/20 alle ore 12:45:32