|Title||Identification and functional expression of the mitochondrial pyruvate carrier.|
|Publication Type||Journal Article|
|Year of Publication||2012|
|Authors||Herzig, S, Raemy, E, Montessuit, S, Veuthey, J-L, Zamboni, N, Westermann, B, Kunji, ERS, Martinou, J-C|
|Date Published||2012 Jul 6|
|Keywords||Amino Acid Sequence, Animals, Anion Transport Proteins, Biological Transport, Biosynthetic Pathways, Culture Media, Lactococcus lactis, Leucine, Mice, Mitochondria, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Molecular Sequence Data, Proprotein Convertase 1, Proprotein Convertase 2, Pyruvic Acid, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Thioctic Acid, Valine|
The transport of pyruvate, the end product of glycolysis, into mitochondria is an essential process that provides the organelle with a major oxidative fuel. Although the existence of a specific mitochondrial pyruvate carrier (MPC) has been anticipated, its molecular identity remained unknown. We report that MPC is a heterocomplex formed by two members of a family of previously uncharacterized membrane proteins that are conserved from yeast to mammals. Members of the MPC family were found in the inner mitochondrial membrane, and yeast mutants lacking MPC proteins showed severe defects in mitochondrial pyruvate uptake. Coexpression of mouse MPC1 and MPC2 in Lactococcus lactis promoted transport of pyruvate across the membrane. These observations firmly establish these proteins as essential components of the MPC.
|Grant List||MC_U105663139 / / Medical Research Council / United Kingdom|