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Titolo:
Phosphorylation of the pro-apoptotic protein BAD on serine 155, a novel site, contributes to cell survival
Autore:
Virdee, K; Parone, PA; Tolkovsky, AM;
Indirizzi:
Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England Univ Cambridge Cambridge England CB2 1QW hem, Cambridge CB2 1QW, England
Titolo Testata:
CURRENT BIOLOGY
fascicolo: 18, volume: 10, anno: 2000,
pagine: 1151 - 1154
SICI:
0960-9822(20000921)10:18<1151:POTPPB>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
SYMPATHETIC NEURONS; KINASE; DEATH; MITOCHONDRIA; ACTIVATION; RAF-1; AKT; BCL-X(L); PATHWAY; SIGNALS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Tolkovsky, AM Univ Cambridge, Dept Biochem, Tennis Court Rd, Cambridge CB21QW, England Univ Cambridge Tennis Court Rd Cambridge England CB2 1QW nd
Citazione:
K. Virdee et al., "Phosphorylation of the pro-apoptotic protein BAD on serine 155, a novel site, contributes to cell survival", CURR BIOL, 10(18), 2000, pp. 1151-1154

Abstract

Phosphorylation of BAD, a pro-apoptotic member of the Bcl-2 protein family, on either Ser112 or Ser136 is thought to be necessary and sufficient for growth factors to promote cell survival. Here we report that Ser155, a sitephosphorylated by protein kinase A (PKA), also contributes to cell survival. Ser112 is thought to be the critical PKA target, but we found that BAD fusion proteins containing Ala at Ser112 (S112A) or Ser136 (S136A) or at both positions (S112/136A) were still heavily phosphorylated by PKA in an in vitro kinase assay. BAD became insensitive to phosphorylation by PKA only when both Ser112 and Ser136, or all three serines (S112/136/155) were mutatedto alanine. In HEK293 cells, BAD fusion proteins mutated at Ser155 were refractory to phosphorylation induced by elevation of cyclic AMP (cAMP) levels. Phosphorylation of the S112/136A mutant was > 90% inhibited by H89, a PKA inhibitor. The S155A mutant induced more apoptosis than the wildtype protein in serum-maintained CHO-K1 cells, and apoptosis induced by the S112/136A mutant was potentiated by serum withdrawal. These data suggest that Ser155 is a major site of phosphorylation by PKA and serum-induced kinases. LikeSer112 and Ser136, phosphorylation of Ser155 contributes to the cancellation of the pro-apoptotic function of BAD.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/08/20 alle ore 20:36:58