Protein kinase B/Akt binds and phosphorylates PED/PEA-15, stabilizing its antiapoptotic action. (Articolo in rivista)

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  • Protein kinase B/Akt binds and phosphorylates PED/PEA-15, stabilizing its antiapoptotic action. (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Trencia A. 1, Perfetti A. 1, Cassese A. 1, Vigliotta G. 1, Miele C. 1, Oriente F. 1, Santopietro S. 1, Giacco F. 1, Condorelli G. 1, Formisano P. 1, Beguinot F. 1 (2003)
    Protein kinase B/Akt binds and phosphorylates PED/PEA-15, stabilizing its antiapoptotic action.
    in Molecular and cellular biology (Print)
    (literal)
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  • Trencia A. 1, Perfetti A. 1, Cassese A. 1, Vigliotta G. 1, Miele C. 1, Oriente F. 1, Santopietro S. 1, Giacco F. 1, Condorelli G. 1, Formisano P. 1, Beguinot F. 1 (literal)
Pagina inizio
  • 4511 (literal)
Pagina fine
  • 4521 (literal)
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  • Impact Factor = 9,836 Interdisciplinarietà del prodotto: The Authors belong to different scientific areas, sectors and Istitutions. (literal)
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  • 23 (literal)
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  • In vitro, recombinant PED/PEA-15 was phosphorylated by Akt with a stoichiometry close to 1. Based on Western blotting with specific phospho-Ser(116) PED/PEA-15 antibodies, Akt phosphorylation of PED/PEA-15 occurred mainly at Ser(116). In addition, a mutant of PED/PEA-15 featuring the substitution of Ser(116)-->Gly (PED(S116-->G)) showed 10-fold-decreased phosphorylation by Akt. In intact 293 cells, Akt also induced phosphorylation of PED/PEA-15 at Ser(116). Serum activation of Akt as well as BAD phosphorylation by Akt showed no difference in 293 cells transfected with PED/PEA-15 and in untransfected cells (which express no endogenous PED/PEA-15). However, the antiapoptotic action of PED/PEA-15 was almost twofold reduced in PED(S116-->G) compared to that in PED/PEA-15(WT) cells. PED/PEA-15 stability closely paralleled Akt activation by serum in 293 cells. In these cells, the nonphosphorylatable PED(S116-->G) mutant exhibited a degradation rate threefold greater than that observed with wild-type PED/PEA-15. In the U373MG glioma cells, blocking Akt also reduced PED/PEA-15 levels and induced sensitivity to tumor necrosis factor-related apoptosis-inducing ligand apoptosis. Thus, phosphorylation by Akt regulates the antiapoptotic function of PED/PEA-15 at least in part by controlling the stability of PED/PEA-15. In part, Akt survival signaling may be mediated by PED/PEA-15. (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • 1 Dipartimento di Biologia e Patologia Cellulare e Molecolare and Istituto di Endocrinologia ed Oncologia Sperimentale del C.N.R., Federico II University of Naples, Naples, Italy. (literal)
Titolo
  • Protein kinase B/Akt binds and phosphorylates PED/PEA-15, stabilizing its antiapoptotic action. (literal)
Abstract
  • The antiapoptotic protein PED/PEA-15 features an Akt phosphorylation motif upstream from Ser(116). In vitro, recombinant PED/PEA-15 was phosphorylated by Akt with a stoichiometry close to 1. Based on Western blotting with specific phospho-Ser(116) PED/PEA-15 antibodies, Akt phosphorylation of PED/PEA-15 occurred mainly at Ser(116). In addition, a mutant of PED/PEA-15 featuring the substitution of Ser(116)-->Gly (PED(S116-->G)) showed 10-fold-decreased phosphorylation by Akt. In intact 293 cells, Akt also induced phosphorylation of PED/PEA-15 at Ser(116). Based on pull-down and coprecipitation assays, PED/PEA-15 specifically bound Akt, independently of Akt activity. Serum activation of Akt as well as BAD phosphorylation by Akt showed no difference in 293 cells transfected with PED/PEA-15 and in untransfected cells (which express no endogenous PED/PEA-15). However, the antiapoptotic action of PED/PEA-15 was almost twofold reduced in PED(S116-->G) compared to that in PED/PEA-15(WT) cells. PED/PEA-15 stability closely paralleled Akt activation by serum in 293 cells. In these cells, the nonphosphorylatable PED(S116-->G) mutant exhibited a degradation rate threefold greater than that observed with wild-type PED/PEA-15. In the U373MG glioma cells, blocking Akt also reduced PED/PEA-15 levels and induced sensitivity to tumor necrosis factor-related apoptosis-inducing ligand apoptosis. Thus, phosphorylation by Akt regulates the antiapoptotic function of PED/PEA-15 at least in part by controlling the stability of PED/PEA-15. In part, Akt survival signaling may be mediated by PED/PEA-15. (literal)
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