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Bcl-2 Phosphorylation by p38 MAPK: identification of target sites and biologic consequences. (Articolo in rivista)

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Bcl-2 Phosphorylation by p38 MAPK: identification of target sites and biologic consequences. (Articolo in rivista) (literal)

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De Chiara G.(1); Marcocci M.E.2; Torcia M.3; Lucibello M.3,4; Rosini P.3; Bonini P.3; Higashimoto Y.5, Damonte G.6; Armirotti A.6; Amodei S.3; Palamara A.T.7; RussoT.8; Garaci E.2; Cozzolino F.3 (2006)
Bcl-2 Phosphorylation by p38 MAPK: identification of target sites and biologic consequences.
in Journal of biological chemistry (Online)
(literal)

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De Chiara G.(1); Marcocci M.E.2; Torcia M.3; Lucibello M.3,4; Rosini P.3; Bonini P.3; Higashimoto Y.5, Damonte G.6; Armirotti A.6; Amodei S.3; Palamara A.T.7; RussoT.8; Garaci E.2; Cozzolino F.3 (literal)

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1 = Department of Cell Biology and Neuroscience, Istituto Superiore di Sanità, Viale Regina Elena 299, I-00161 Rome, Italy; 2 = Department of Experimental Medicine and Biochemical Sciences, University of Rome \"Tor Vergata\", Via Montpellier 1, I-00133 Rome, Italy; 3 = Department of Clinical Physiopathology, University of Florence, Viale Pieraccini 6, I-50139 Florence, Italy; 4 = Institute of Neurobiology and Molecular Medicine, National Research Council, Via Fosso del Cavaliere 100, I-00133 Rome, Italy; 5 = Laboratory of Cell Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892 6 = DIMES Biochemistry Section, Mass Spectrometry Facility, Center of Excellence for Biomedical Research, University of Genoa, Viale Benedetto XV 7, I-16132 Genoa, Italy; 7 = Department of Public Health Science \"G. Sanarelli,\" University of Rome \"La Sapienza,\" Piazzale A. Moro 5, I-00185 Rome, Italy; 8 = CEINGE Biotecnologie Avanzate, Department of Biochemistry and Medical Biotechnologies, University of Naples \"Federico II,\" Via Comunale Margherita 482, I-80131 Naples, Italy (literal)

Titolo

Bcl-2 Phosphorylation by p38 MAPK: identification of target sites and biologic consequences. (literal)

Abstract

The antiapoptotic role of Bcl-2 can be regulated by its phosphorylation in serine and threonine residues located in a nonstructured loop that links BH3 and BH4 domains. p38 MAPK has been identified as one of the kinases able to mediate such phosphorylation, through direct interaction with Bcl-2 protein in the mitochondrial compartment. In this study, we identify, by using mass spectrometry techniques and specific anti-phosphopeptide antibodies, Ser(87) and Thr(56) as the Bcl-2 residues phosphorylated by p38 MAPK and show that phosphorylation of these residues is always associated with a decrease in the antiapoptotic potential of Bcl-2 protein. Furthermore, we obtained evidence that p38 MAPK-induced Bcl-2 phosphorylation plays a key role in the early events following serum deprivation in embryonic fibroblasts. Both cytochrome c release and caspase activation triggered by p38 MAPK activation and Bcl-2 phosphorylation are absent in embryonic fibroblasts from p38alpha knock-out mice (p38alpha(-/-) MEF), whereas they occur within 12 h of serum withdrawal in p38alpha(+/+) MEF; moreover, they can be prevented by p38 MAPK inhibitors and are not associated with the synthesis of the proapoptotic proteins Bax and Fas. Thus, Bcl-2 phosphorylation by activated p38 MAPK is a key event in the early induction of apoptosis under conditions of cellular stress. (literal)

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