Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1774, Issue 5, Pages 628-636Publisher
ELSEVIER
DOI: 10.1016/j.bbapap.2007.03.012
Keywords
carnitine palmitoyltransferase-I; long chain acyl-CoA synthetase; voltage dependent anion channel; post-translational modifications; mitochondria
Categories
Funding
- NIA NIH HHS [P01 AG015885, P01 AG015885-070004, P01 AG015885-079003, P01 AG15885, P01 AG015885-07] Funding Source: Medline
- NIDDK NIH HHS [R01 DK066107, DK-0071319-26, R01 DK066107-02, DK-066107] Funding Source: Medline
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The identification of post-translational modifications is difficult especially for hydrophobic membrane proteins. Here we present the identification of several types of protein modifications on membrane proteins isolated from mitochondrial outer membranes. We show, in vivo, that the mature rat liver mitochondrial carnitine palmitoyltransferase-I enzyme is N-terminally acetylated, phosphorylated on two threonine residues, and nitrated on two tyrosine residues. We show that long chain acyl-CoA synthetase I is acetylated at both the N-terminal end and at a lysine residue and tyrosine residues are found to be phosphorylated and nitrated. For the three voltage-dependent anion channel isoforms present in the mitochondria, the N-terminal regions of the protein were determined and sites of phosphorylation were identified. These novel findings raise questions about regulatory aspects of carnitine palmitoyltransferase-I, long chain acyl-CoA synthetase and voltage dependent anion channel and further studies should advance our understanding about regulation of mitochondrial fatty acid oxidation in general and these three proteins in specific. (C) 2007 Elsevier B.V. All rights reserved.
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