Omi/HtrA2 promotes cell death by binding and degrading the antiapoptotic protein PED/PEA-15. (Articolo in rivista)

Type
Label
  • Omi/HtrA2 promotes cell death by binding and degrading the antiapoptotic protein PED/PEA-15. (Articolo in rivista) (literal)
Anno
  • 2004-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1074/jbc.M406317200 (literal)
Alternative label
  • Trencia A., Fiory F., Maitan M.A., Vito P., Barbagallo A.P.M., Perfetti A., Miele C., Ungaro P., Oriente F., Cilenti L., Zervos A.S., Formisano P. and Beguinot F. (2004)
    Omi/HtrA2 promotes cell death by binding and degrading the antiapoptotic protein PED/PEA-15.
    in Journal of biological chemistry (Online)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Trencia A., Fiory F., Maitan M.A., Vito P., Barbagallo A.P.M., Perfetti A., Miele C., Ungaro P., Oriente F., Cilenti L., Zervos A.S., Formisano P. and Beguinot F. (literal)
Pagina inizio
  • 46566 (literal)
Pagina fine
  • 46572 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 279 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 45 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento di Biologia e Patologia Cellulare e Molecolare and Istituto di Endocrinologia ed Oncologia Sperimentale del CNR, Universita` degli Studi di Napoli Federico II, Naples 80131, Italy, Dipartimento di Scienze Biologiche ed Ambientali, Universita` degli Studi del Sannio, Benevento 82100, Italy, and the Department of Molecular Biology and Microbiology, University of Central Florida, Orlando, Florida 32826 (literal)
Titolo
  • Omi/HtrA2 promotes cell death by binding and degrading the antiapoptotic protein PED/PEA-15. (literal)
Abstract
  • ped/pea-15 is a ubiquitously expressed 15-kDa protein featuring a broad anti-apoptotic function. In a yeast two-hybrid screen, the pro-apoptotic Omi/HtrA2 mitochondrial serine protease was identified as a specific interactor of the ped/pea-15 death effector domain. Omi/HtrA2 also bound recombinant ped/pea-15 in vitro and co-precipitated with ped/pea-15 in 293 and HeLa cell extracts. In these cells, the binding of Omi/HtrA2 to ped/pea-15 was induced by UVC exposure and followed the mitochondrial release of Omi/HtrA2 into the cytoplasm. Upon UVC exposure, cellular ped/pea-15 protein expression levels decreased. This effect was prevented by the ucf-101 specific inhibitor of the Omi/HtrA2 proteolytic activity, in a dose-dependent fashion. In vitro incubation of ped/pea-15 with Omi/HtrA2 resulted in ped/pea-15 degradation. In intact cells, the inhibitory action of ped/pea-15 on UVC-induced apoptosis progressively declined at increasing Omi/HtrA2 expression. This further effect of Omi/HtrA2 was also inhibited by ucf-101. In addition, ped/pea-15 expression blocked Omi/HtrA2 co-precipitation with the caspase inhibitor protein XIAP and caspase 3 activation. Thus, in part, apoptosis following Omi/HtrA2 mitochondrial release is mediated by reduction in ped/pea-15 cellular levels. The ability of Omi/HtrA2 to relieve XIAP inhibition on caspases is modulated by the relative levels of Omi/HtrA2 and ped/pea-15. (literal)
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