A Mitochondrial Pyruvate Carrier Required for Pyruvate Uptake in Yeast, Drosophila, and Humans
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 membran...
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| Published in | Science (American Association for the Advancement of Science) Vol. 337; no. 6090; pp. 96 - 100 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Washington, DC
American Association for the Advancement of Science
06.07.2012
The American Association for the Advancement of Science |
| Subjects | |
| Online Access | Get full text |
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| Abstract | 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 and a depletion of tricarboxylic acid cycle intermediates. Loss of yeast Mpc1 results in defective mitochondrial pyruvate uptake, and silencing of MPC1 or MPC2 in mammalian cells impairs pyruvate oxidation. A point mutation in MPC1 provides resistance to a known inhibitor of the mitochondrial pyruvate carrier. Human genetic studies of three families with children suffering from lactic acidosis and hyperpyruvatemia revealed a causal locus that mapped to MPC1, changing single amino acids that are conserved throughout eukaryotes. These data demonstrate that Mpc1 and Mpc2 form an essential part of the mitochondrial pyruvate carrier. |
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| AbstractList | 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 and a depletion of tricarboxylic acid cycle intermediates. Loss of yeast Mpc1 results in defective mitochondrial pyruvate uptake, and silencing of MPC1 or MPC2 in mammalian cells impairs pyruvate oxidation. A point mutation in MPC1 provides resistance to a known inhibitor of the mitochondrial pyruvate carrier. Human genetic studies of three families with children suffering from lactic acidosis and hyperpyruvatemia revealed a causal locus that mapped to MPC1, changing single amino acids that are conserved throughout eukaryotes. These data demonstrate that Mpc1 and Mpc2 form an essential part of the mitochondrial pyruvate carrier. 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 and a depletion of tricarboxylic acid cycle intermediates. Loss of yeast Mpc1 results in defective mitochondrial pyruvate uptake, and silencing of MPC1 or MPC2 in mammalian cells impairs pyruvate oxidation. A point mutation in MPC1 provides resistance to a known inhibitor of the mitochondrial pyruvate carrier. Human genetic studies of three families with children suffering from lactic acidosis and hyperpyruvatemia revealed a causal locus that mapped to MPC1 , changing single amino acids that are conserved throughout eukaryotes. These data demonstrate that Mpc1 and Mpc2 form an essential part of the mitochondrial pyruvate carrier. Letting Pyruvate InTransport of pyruvate is an important event in metabolism whereby the pyruvate formed in glycolysis is transported into mitochondria to feed into the tricarboxylic acid cycle (see the Perspective by Murphy and Divakaruni). Two groups have now identified proteins that are components of the mitochondrial pyruvate transporter. Bricker et al. (p. 96, published online 24 May) found that the proteins mitochondrial pyruvate carrier 1 and 2 (MPC1 and MPC2) are required for full pyruvate transport in yeast and Drosophila cells and that humans with mutations in MPC1 have metabolic defects consistent with loss of the transporter. Herzig et al. (p. 93, published online 24 May) identified the same proteins as components of the carrier in yeast. Furthermore, expression of the mouse proteins in bacteria conferred increased transport of pyruvate into bacterial cells. Letting Pyruvate In Transport of pyruvate is an important event in metabolism whereby the pyruvate formed in glycolysis is transported into mitochondria to feed into the tricarboxylic acid cycle (see the Perspective by Murphy and Divakaruni). Two groups have now identified proteins that are components of the mitochondrial pyruvate transporter. Bricker et al. (p. 96, published online 24 May) found that the proteins mitochondrial pyruvate carrier 1 and 2 (MPC1 and MPC2) are required for full pyruvate transport in yeast and Drosophila cells and that humans with mutations in MPC1 have metabolic defects consistent with loss of the transporter. Herzig et al. (p. 93, published online 24 May) identified the same proteins as components of the carrier in yeast. Furthermore, expression of the mouse proteins in bacteria conferred increased transport of pyruvate into bacterial cells. 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 and a depletion of tricarboxylic acid cycle intermediates. Loss of yeast Mpc1 results in defective mitochondrial pyruvate uptake, and silencing of MPC1 or MPC2 in mammalian cells impairs pyruvate oxidation. A point mutation in MPC1 provides resistance to a known inhibitor of the mitochondrial pyruvate carrier. Human genetic studies of three families with children suffering from lactic acidosis and hyperpyruvatemia revealed a causal locus that mapped to MPC1, changing single amino acids that are conserved throughout eukaryotes. These data demonstrate that Mpc1 and Mpc2 form an essential part of the mitochondrial pyruvate carrier.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 and a depletion of tricarboxylic acid cycle intermediates. Loss of yeast Mpc1 results in defective mitochondrial pyruvate uptake, and silencing of MPC1 or MPC2 in mammalian cells impairs pyruvate oxidation. A point mutation in MPC1 provides resistance to a known inhibitor of the mitochondrial pyruvate carrier. Human genetic studies of three families with children suffering from lactic acidosis and hyperpyruvatemia revealed a causal locus that mapped to MPC1, changing single amino acids that are conserved throughout eukaryotes. These data demonstrate that Mpc1 and Mpc2 form an essential part of the mitochondrial pyruvate carrier. Transport of pyruvate is an important event in metabolism whereby the pyruvate formed in glycolysis is transported into mitochondria to feed into the tricarboxylic acid cycle (see the Perspective by Murphy and Divakaruni ). Two groups have now identified proteins that are components of the mitochondrial pyruvate transporter. Bricker et al. (p. 96, published online 24 May) found that the proteins mitochondrial pyruvate carrier 1 and 2 (MPC1 and MPC2) are required for full pyruvate transport in yeast and Drosophila cells and that humans with mutations in MPC1 have metabolic defects consistent with loss of the transporter. Herzig et al. (p. 93, published online 24 May) identified the same proteins as components of the carrier in yeast. Furthermore, expression of the mouse proteins in bacteria conferred increased transport of pyruvate into bacterial cells. 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 and a depletion of tricarboxylic acid cycle intermediates. Loss of yeast Mpc1 results in defective mitochondrial pyruvate uptake, and silencing of MPC1 or MPC2 in mammalian cells impairs pyruvate oxidation. A point mutation in MPC1 provides resistance to a known inhibitor of the mitochondrial pyruvate carrier. Human genetic studies of three families with children suffering from lactic acidosis and hyperpyruvatemia revealed a causal locus that mapped to MPC1, changing single amino acids that are conserved throughout eukaryotes. These data demonstrate that Mpc1 and Mpc2 form an essential part of the mitochondrial pyruvate carrier. [PUBLICATION ABSTRACT] Transport of pyruvate is an important event in metabolism whereby the pyruvate formed in glycolysis is transported into mitochondria to feed into the tricarboxylic acid cycle (see the Perspective by Murphy and Divakaruni ). Two groups have now identified proteins that are components of the mitochondrial pyruvate transporter. Bricker et al. (p. 96 , published online 24 May) found that the proteins mitochondrial pyruvate carrier 1 and 2 (MPC1 and MPC2) are required for full pyruvate transport in yeast and Drosophila cells and that humans with mutations in MPC1 have metabolic defects consistent with loss of the transporter. Herzig et al. (p. 93 , published online 24 May) identified the same proteins as components of the carrier in yeast. Furthermore, expression of the mouse proteins in bacteria conferred increased transport of pyruvate into bacterial cells. The genes encoding two components of the pyruvate transporter in mitochondria have been identified. 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 and a depletion of tricarboxylic acid cycle intermediates. Loss of yeast Mpc1 results in defective mitochondrial pyruvate uptake, and silencing of MPC1 or MPC2 in mammalian cells impairs pyruvate oxidation. A point mutation in MPC1 provides resistance to a known inhibitor of the mitochondrial pyruvate carrier. Human genetic studies of three families with children suffering from lactic acidosis and hyperpyruvatemia revealed a causal locus that mapped to MPC1 , changing single amino acids that are conserved throughout eukaryotes. These data demonstrate that Mpc1 and Mpc2 form an essential part of the mitochondrial pyruvate carrier. |
| Author | Schell, John C. Bricker, Daniel K. Orsak, Thomas Boudina, Sihem Cox, James E. Thummel, Carl S. Gygi, Steven P. Chen, Yu-Chan Brivet, Michèle Rutter, Jared Taylor, Eric B. Van Vranken, Jonathan G. Redin, Claire Boutron, Audrey Cardon, Caleb M. Dephoure, Noah |
| AuthorAffiliation | 4 Metabolomics Core Research Facility, University of Utah School of Medicine, Salt Lake City, UT 84112, USA 6 Institut de Genetique et de Biologie Moleculaire et Cellulaire (IGBMC), Strasbourg, France 1 Department of Human Genetics, University of Utah School of Medicine, Salt Lake City, UT 84112, USA 3 Laboratoire de Biochimie, AP-HP Hôpital de Bicêtre, Le Kremlin Bicêtre, France 5 Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA 7 Department of Medicine, University of Utah School of Medicine, Salt Lake City, UT 84112, USA 2 Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112, USA |
| AuthorAffiliation_xml | – name: 1 Department of Human Genetics, University of Utah School of Medicine, Salt Lake City, UT 84112, USA – name: 2 Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112, USA – name: 6 Institut de Genetique et de Biologie Moleculaire et Cellulaire (IGBMC), Strasbourg, France – name: 7 Department of Medicine, University of Utah School of Medicine, Salt Lake City, UT 84112, USA – name: 3 Laboratoire de Biochimie, AP-HP Hôpital de Bicêtre, Le Kremlin Bicêtre, France – name: 5 Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA – name: 4 Metabolomics Core Research Facility, University of Utah School of Medicine, Salt Lake City, UT 84112, USA |
| Author_xml | – sequence: 1 givenname: Daniel K. surname: Bricker fullname: Bricker, Daniel K. – sequence: 2 givenname: Eric B. surname: Taylor fullname: Taylor, Eric B. – sequence: 3 givenname: John C. surname: Schell fullname: Schell, John C. – sequence: 4 givenname: Thomas surname: Orsak fullname: Orsak, Thomas – sequence: 5 givenname: Audrey surname: Boutron fullname: Boutron, Audrey – sequence: 6 givenname: Yu-Chan surname: Chen fullname: Chen, Yu-Chan – sequence: 7 givenname: James E. surname: Cox fullname: Cox, James E. – sequence: 8 givenname: Caleb M. surname: Cardon fullname: Cardon, Caleb M. – sequence: 9 givenname: Jonathan G. surname: Van Vranken fullname: Van Vranken, Jonathan G. – sequence: 10 givenname: Noah surname: Dephoure fullname: Dephoure, Noah – sequence: 11 givenname: Claire surname: Redin fullname: Redin, Claire – sequence: 12 givenname: Sihem surname: Boudina fullname: Boudina, Sihem – sequence: 13 givenname: Steven P. surname: Gygi fullname: Gygi, Steven P. – sequence: 14 givenname: Michèle surname: Brivet fullname: Brivet, Michèle – sequence: 15 givenname: Carl S. surname: Thummel fullname: Thummel, Carl S. – sequence: 16 givenname: Jared surname: Rutter fullname: Rutter, Jared |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26103649$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/22628558$$D View this record in MEDLINE/PubMed https://hal.science/hal-04299019$$DView record in HAL |
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| Keywords | Ascomycota Human Yeast Cell organelle Insecta Biological transport Pyruvate Drosophilidae Fungi Transport process Mitochondria Arthropoda Carboxylate Invertebrata Drosophila melanogaster Saccharomyces cerevisiae Diptera |
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| Snippet | Pyruvate constitutes a critical branch point in cellular carbon metabolism. We have identified two proteins, Mpc1 and Mpc2, as essential for mitochondrial... Transport of pyruvate is an important event in metabolism whereby the pyruvate formed in glycolysis is transported into mitochondria to feed into the... Letting Pyruvate InTransport of pyruvate is an important event in metabolism whereby the pyruvate formed in glycolysis is transported into mitochondria to feed... Letting Pyruvate In Transport of pyruvate is an important event in metabolism whereby the pyruvate formed in glycolysis is transported into mitochondria to... |
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| SubjectTerms | Amino Acid Sequence Amino acids Amino Acids - metabolism Animals Anion Transport Proteins - chemistry Anion Transport Proteins - genetics Anion Transport Proteins - metabolism Bacteria Biochemistry, Molecular Biology Biological and medical sciences Biological Transport Carbohydrate Metabolism Carriers Cell physiology Citric Acid Cycle Diet Drosophila Drosophila melanogaster - chemistry Drosophila melanogaster - genetics Drosophila melanogaster - metabolism Drosophila Proteins - chemistry Drosophila Proteins - genetics Drosophila Proteins - metabolism Fundamental and applied biological sciences. Psychology glycolysis Human Humans Life Sciences Medical schools Membrane and intracellular transports Metabolism Metabolites Metabolomics mice Mitochondria Mitochondria - metabolism Mitochondrial Membrane Transport Proteins - chemistry Mitochondrial Membrane Transport Proteins - genetics Mitochondrial Membrane Transport Proteins - metabolism Mitochondrial Membranes - metabolism Mitochondrial Proteins - chemistry Mitochondrial Proteins - genetics Mitochondrial Proteins - metabolism Molecular and cellular biology Molecular Sequence Data Mutation Oxidation Oxidation-Reduction Plasmids Point Mutation Proteins Pyruvates pyruvic acid Pyruvic Acid - metabolism Respiration Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Sugars Transport Transporter tricarboxylic acid cycle Yeast Yeasts |
| Title | A Mitochondrial Pyruvate Carrier Required for Pyruvate Uptake in Yeast, Drosophila, and Humans |
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