Identification of tyrosine-phosphorylated proteins of the mitochondrial oxidative phosphorylation machinery |
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Authors: | O. Augereau S. Claverol N. Boudes M.-J. Basurko M. Bonneu R. Rossignol J.-P. Mazat T. Letellier J. Dachary-Prigent |
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Affiliation: | (1) Physiopathologie Mitochondriale, INSERM U688, Université Victor Segalen-Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux-Cedex, France;(2) Pôle Protéomique, Plateforme Génomique Fonctionnelle Bordeaux, Université Victor Segalen-Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux-Cedex, France;(3) Laboratoire de Biochimie Médicale, Université Victor Segalen-Bordeaux 2, 146 rue Léo Saignat, 33 076 Bordeaux-Cedex, France |
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Abstract: | The role of some serine/threonine kinases in the regulation of mitochondrial physiology is now well established, but little is known about mitochondrial tyrosine kinases. We showed that tyrosine phosphorylation of rat brain mitochondrial proteins was increased by in vitro addition of ATP and H2O2, and also during in situ ATP production at state 3, and maximal reactive oxygen species production. The Src kinase inhibitor PP2 decreased tyrosine phosphorylation and respiratory rates at state 3. We found that the 39-kDa subunit of complex I was tyrosine phosphorylated, and we identified putative tyrosine-phosphorylated subunits for the other complexes. We also have strong evidence that the FoF1-ATP synthase α chain is probably tyrosine-phosphorylated, but demonstrated that the β chain is not. The tyrosine phosphatase PTP 1B was found in brain but not in muscle, heart or liver mitochondria. Our results suggest that tyrosine kinases and phosphatases are involved in the regulation of oxidative phosphorylation.Received 7 January 2005; received after revision 19 April 2005; accepted 22 April 2005 |
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Keywords: | Mitochondria oxidative phosphorylation tyrosine phosphorylation Src kinase PTP 1B oxidant |
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