Identification of new tyrosine phosphorylated proteins in rat brain mitochondria

Lewandrowski, Urs; Sickmann, Albert; Cesaro, Luca; Brunati, Anna Maria; Toninello, Antonio; Salvi, Mauro

doi:10.1016/j.febslet.2008.02.077

« Previous Next »FEBS Letters
Volume 582, Issue 7 , Pages 1104-1110, 2 April 2008

Identification of new tyrosine phosphorylated proteins in rat brain mitochondria

Edited by Giulio Superti-Fürga

Urs Lewandrowski
- Protein Mass Spectrometry and Functional Proteomics Group, Rudolf-Virchow-Center for Experimental Biomedicine, Versbacher Strasse 9, 97078 Würzburg, Germany
Albert Sickmann
- Protein Mass Spectrometry and Functional Proteomics Group, Rudolf-Virchow-Center for Experimental Biomedicine, Versbacher Strasse 9, 97078 Würzburg, Germany
Luca Cesaro
- Department of Biological Chemistry, University of Padova, Viale G. Colombo 3, 35121 Padova, Italy
Anna Maria Brunati
- Department of Biological Chemistry, University of Padova, Viale G. Colombo 3, 35121 Padova, Italy
Antonio Toninello
- Department of Biological Chemistry, University of Padova, Viale G. Colombo 3, 35121 Padova, Italy
Mauro Salvi
- Department of Biological Chemistry, University of Padova, Viale G. Colombo 3, 35121 Padova, Italy
- Corresponding author. Fax: +39 0498073310.

Received 10 December 2007; received in revised form 12 February 2008; accepted 29 February 2008. published online 10 March 2008.

Abstract

Reversible protein-phosphorylation is emerging as a key player in the regulation of mitochondrial functions. In particular tyrosine phosphorylation represents a promising field to highlight new mechanisms of bioenergetic regulation.

Utilizing immunoaffinity enrichment of phosphotyrosine-containing peptides coupled to mass spectrometric analysis we detected new tyrosine phosphorylated proteins in rat brain mitochondria after peroxovanadate treatment. By bioinformatic predictions we provide suggestions about the potential role of tyrosine phosphorylation in mitochondrial physiology. Our results indicate a primary role of tyrosine phosphorylation in regulating energy production at the mitochondrial level. Moreover, tyrosine phosphorylation might regulate the mitochondrial membrane permeability targeting protein complexes containing ADP/ATP translocase, VDAC, creatine kinase and hexokinase.

Keywords: Mitochondria, Tyrosine phosphorylated protein, Rat brain, Energy production, Membrane permeabilization

Abbreviations: ANT, ADP/ATP translocase, COX, cytochrome c oxidase, mtCK, mitochondrial creatine kinase, ETC, electron-transport chain, HK-I, Type I hexokinase, MPT, mitochondrial permeability transition, PTPM-1, protein tyrosine phosphatase localized to the mitochondrion 1, RBM, rat brain mitochondria, VDAC, voltage-dependent anion channel