Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) phosphorylation by protein kinase Cδ (PKCδ) inhibits mitochondria elimination by lysosomal-like structures following ischemia and reoxygenation-induced injury
Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
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Data(s) |
28/03/2014
28/03/2014
28/06/2013
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Resumo |
Background: How damaged mitochondria are removed by mitophagy is not fully described. Results: Ischemia and reoxygenation (I/R)-induced injury triggers mitochondria association of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and mitophagy, and protein kinase Cδ (PKCδ) activation inhibits it. Conclusion: PKCδ-mediated phosphorylation of GAPDH inhibits mitophagy. Significance: GAPDH/PKCδ is a signaling switch, which is activated during ischemic injury to regulate the balance between cell survival by mitophagy and cell death by apoptosis. National Institutes of Health Grant HL052141 |
Identificador |
Journal of Biological Chemistry, Baltimore, v.288, n.26, p.18947-18960, 2013 http://www.producao.usp.br/handle/BDPI/44318 10.1074/jbc.M113.466870 |
Idioma(s) |
eng |
Publicador |
American Society for Biochemistry and Molecular Biology Baltimore |
Relação |
Journal of Biological Chemistry |
Direitos |
restrictedAccess The American Society for Biochemistry and Molecular Biology, Inc. |
Palavras-Chave | #Mitocôndrias #Isquemia #Apoptose |
Tipo |
article original article publishedVersion |