BAIT

MPC1

FMP37, YGL080W
Highly conserved subunit of the mitochondrial pyruvate carrier; a mitochondrial inner membrane complex comprised of Mpc1p and either Mpc2p or Mpc3p mediates mitochondrial pyruvate uptake; null mutant displays slow growth that is complemented by expression of human or mouse ortholog; mutation in human ortholog is associated with lactic acidosis and hyperpyruvatemia
GO Process (0)
GO Function (0)
GO Component (0)
Saccharomyces cerevisiae (S288c)
PREY

MGR3

FMP24, YMR115W
Subunit of the mitochondrial (mt) i-AAA protease supercomplex; i-AAA degrades misfolded mitochondrial proteins; forms a subcomplex with Mgr1p that binds to substrates to facilitate proteolysis; required for growth of cells lacking mtDNA
GO Process (1)
GO Function (1)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

A Mitochondrial Pyruvate Carrier Required for Pyruvate Uptake in Yeast, Drosophila, and Humans.

Bricker DK, Taylor EB, Schell JC, Orsak T, Boutron A, Chen YC, Cox JE, Cardon CM, Van Vranken JG, Dephoure N, Redin C, Boudina S, Gygi SP, Brivet M, Thummel CS, Rutter J

Pyruvate constitutes a critical branch point in cellular carbon metabolism. We have identified two proteins, Mpc1 and Mpc2, as essential for mitochondrial pyruvate transport in yeast, Drosophila, and humans. Mpc1 and Mpc2 associate to form an ~150 kilodalton complex in the inner mitochondrial membrane. Yeast and Drosophila mutants lacking MPC1 display impaired pyruvate metabolism, with an accumulation of upstream metabolites ... [more]

Unknown May. 24, 2012; 0(0); [Pubmed: 22628558]

Throughput

  • Low Throughput

Curated By

  • BioGRID