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Identification of new tyrosine phosphorylated proteins in rat brain mitochondria
Author(s) -
Lewandrowski Urs,
Sickmann Albert,
Cesaro Luca,
Brunati Anna Maria,
Toninello Antonio,
Salvi Mauro
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.02.077
Subject(s) - tyrosine phosphorylation , phosphorylation , voltage dependent anion channel , protein phosphorylation , tyrosine , protein tyrosine phosphatase , mitochondrion , biochemistry , microbiology and biotechnology , biology , atp–adp translocase , hexokinase , chemistry , inner mitochondrial membrane , protein kinase a , glycolysis , metabolism , bacterial outer membrane , escherichia coli , gene
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.