http://rutter.biochem.utah.edu/the-connection-between-metabolism-and-cellular-behaviors daily 0.75 2019-05-22 https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1542673141965-WAC1RGDX8RMPT6YKOSCF/Picture1.png The connection between metabolism and cellular behaviors https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1553893186746-FTWSB39FGL1PF2JRTJ6C/image-asset.jpeg The connection between metabolism and cellular behaviors - Metabolic underpinnings of cancer and stem cells Our discovery of the Mitochondrial Pyruvate Carrier (MPC) has led to the initiation of a significant effort in the lab to understand the fundamental metabolic underpinnings of cancer and stem cells. Modulation of pyruvate metabolism via chemical or genetic manipulation of the MPC has profound effects on intestinal stem cell function and proliferation as well as on cancer metabolism, supporting the idea that metabolism is not merely a by-product but rather an intrinsic driving force of cell fate. We are currently extending these studies using mouse models of human diseases including colon cancer and heart failure. https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1553893267316-TDO50D78PF0A6CAYT7KG/bi-2011-01313s_0003.gif The connection between metabolism and cellular behaviors - MIDAS Small molecule allostery modifies protein function but is not easily discoverable. We have developed an experimental platform - mass spectrometry integrated with equilibrium dialysis for the discovery of allostery systematically (MIDAS) - that enables the identification of physiologically relevant, low-affinity metabolite-protein interactions using unmodified proteins and complex mixtures of unmodified metabolites. Our latest iteration of MIDAS enables high-throughput identification of the allesterome of purified proteins to uncover novel aspects of biology. https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1554240589511-IQVM7SAG2YJ4I9V5NCM9/elife-17985-fig1.jpg The connection between metabolism and cellular behaviors - PASK PAS domain containing protein kinase (Pask) is an evolutionarily conserved, nutrient-sensing serine/threonine protein kinase implicated in energy homeostasis and metabolic regulation across eukaryotic species. We recently described an unexpected role for Pask in regulating the differentiation of stem and progenitor cells into neuronal, adipocytes, and myocytes lineages. Subsequent work has shown that Pask is an interacting partner and a direct substrate of mTORC1, and that is a necessary mediator of the alterations in epigenetic markers that drive muscle cell differentiation in response to nutrient and hormonal signals. https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1553893186746-FTWSB39FGL1PF2JRTJ6C/image-asset.jpeg The connection between metabolism and cellular behaviors - Metabolic underpinnings of cancer and stem cells Our discovery of the Mitochondrial Pyruvate Carrier (MPC) has led to the initiation of a significant effort in the lab to understand the fundamental metabolic underpinnings of cancer and stem cells. Modulation of pyruvate metabolism via chemical or genetic manipulation of the MPC has profound effects on intestinal stem cell function and proliferation as well as on cancer metabolism, supporting the idea that metabolism is not merely a by-product but rather an intrinsic driving force of cell fate. We are currently extending these studies using mouse models of human diseases including colon cancer and heart failure. https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1553893267316-TDO50D78PF0A6CAYT7KG/bi-2011-01313s_0003.gif The connection between metabolism and cellular behaviors - MIDAS Small molecule allostery modifies protein function but is not easily discoverable. We have developed an experimental platform - mass spectrometry integrated with equilibrium dialysis for the discovery of allostery systematically (MIDAS) - that enables the identification of physiologically relevant, low-affinity metabolite-protein interactions using unmodified proteins and complex mixtures of unmodified metabolites. Our latest iteration of MIDAS enables high-throughput identification of the allesterome of purified proteins to uncover novel aspects of biology. https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1554240589511-IQVM7SAG2YJ4I9V5NCM9/elife-17985-fig1.jpg The connection between metabolism and cellular behaviors - PASK PAS domain containing protein kinase (Pask) is an evolutionarily conserved, nutrient-sensing serine/threonine protein kinase implicated in energy homeostasis and metabolic regulation across eukaryotic species. We recently described an unexpected role for Pask in regulating the differentiation of stem and progenitor cells into neuronal, adipocytes, and myocytes lineages. Subsequent work has shown that Pask is an interacting partner and a direct substrate of mTORC1, and that is a necessary mediator of the alterations in epigenetic markers that drive muscle cell differentiation in response to nutrient and hormonal signals. http://rutter.biochem.utah.edu/functionalizing-the-mitochondrial-proteome-1 daily 0.75 2019-05-07 https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1542673118591-IFIYKBGT25TLT3ZYKQ1V/Picture1.jpg Functionalizing the Mitochondrial Proteome https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1553890668503-R1OAB7BZ3JWSV2YHQ5Q0/cover.tif.jpg Functionalizing the Mitochondrial Proteome - Mitochondrial Pyruvate Carrier The fate of pyruvate is one of the most important metabolic decisions made by eukaryotic cells. Most normal, differentiated mammalian cells partition pyruvate primarily toward transport into mitochondria where it is oxidized for efficient ATP production. The partitioning of pyruvate in stem cells, cancer cells, and failing hearts, however, is different—away from mitochondrial oxidation. Our ability to understand the molecular basis for these metabolic distinctions has been hampered by the surprising fact that the mitochondrial pyruvate transporter had not been identified until now. We discovered a protein complex consisting of Mpc1 and Mpc2 that constitutes the major mitochondrial pyruvate transporter in yeast, Drosophila, and humans. Empowered by this discovery, we found that three families with children suffering from lactic acidosis and hyperpyruvatemia had causal mutations in MPC1. https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1553890958052-3I7Q0INKNUNSHCNWZHFE/1-s2.0-S0960982218310674-gr1.jpg Functionalizing the Mitochondrial Proteome - MitoFAS We demonstrated that the mitochondrial acyl carrier protein (ACP), which has a well-known role in mitochondrial fatty acid synthesis (mitoFAS), plays an unexpected and evolutionarily conserved role in FeS biogenesis. Subsequent work, highlighted the role of mitoFAS as a nutrient-sensitive pathway that provides an elegant mechanism whereby acetyl-CoA regulates its own consumption via coordination of lipoic acid synthesis and tricarboxylic acid (TCA) cycle activity, iron-sulfur (FeS) cluster biogenesis, assembly of oxidative phosphorylation complexes, and mitochondrial translation. https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1553890994315-1XIGVQG4TVFQRPK3NBQQ/41467_2018_4564_Fig3_HTML.jpg Functionalizing the Mitochondrial Proteome - Mitochondrial Protein Quality Control Msp1/ATAD1 is a AAA-ATPase protein that we found to reside on the mitochondrial outer membrane. Through a combination of genetics and biochemistry, we showed that it extracts proteins that mis-localize to the mitochondrial outer membrane, which we observed as a surprisingly common phenomenon. We demonstrated this function for the protein family in yeast, human cells, and knockout mice. We found that Vms1 is required for the stress-responsive mitochondrial recruitment of Cdc48/VCP/p97 and Npl4, which play a role in protein extraction and degradation. Further studies led to the conclusion that Vms1 is a critical component of a previously unknown system for mitochondrial protein quality control, eliminating damaged or misfolded proteins that promote progressive mitochondrial dysfunction. https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1553891158993-O412CKMX0CUPVN3LYSOF/nihms600712f1.jpg Functionalizing the Mitochondrial Proteome - Regulation of Electron Transport Chain Assembly We found that both Sdh5 and Sdh8 are required for the assembly of the succinate dehydrogenase complex (Complex II) of the electron transport chain. As a result of these mechanistic functional studies, we were able to discover that familial mutations in human SDH5 (SDHAF2) cause a paraganglioma tumor syndrome. We also discovered a role for Rcf1 in the normal assembly of respiratory supercomplexes in yeast and mammals. Deletion of the RCF1 gene caused impaired respiration and elevated mitochondrial oxidative stress and damage. https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1553890668503-R1OAB7BZ3JWSV2YHQ5Q0/cover.tif.jpg Functionalizing the Mitochondrial Proteome - Mitochondrial Pyruvate Carrier The fate of pyruvate is one of the most important metabolic decisions made by eukaryotic cells. Most normal, differentiated mammalian cells partition pyruvate primarily toward transport into mitochondria where it is oxidized for efficient ATP production. The partitioning of pyruvate in stem cells, cancer cells, and failing hearts, however, is different—away from mitochondrial oxidation. Our ability to understand the molecular basis for these metabolic distinctions has been hampered by the surprising fact that the mitochondrial pyruvate transporter had not been identified until now. We discovered a protein complex consisting of Mpc1 and Mpc2 that constitutes the major mitochondrial pyruvate transporter in yeast, Drosophila, and humans. Empowered by this discovery, we found that three families with children suffering from lactic acidosis and hyperpyruvatemia had causal mutations in MPC1. https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1553890958052-3I7Q0INKNUNSHCNWZHFE/1-s2.0-S0960982218310674-gr1.jpg Functionalizing the Mitochondrial Proteome - MitoFAS We demonstrated that the mitochondrial acyl carrier protein (ACP), which has a well-known role in mitochondrial fatty acid synthesis (mitoFAS), plays an unexpected and evolutionarily conserved role in FeS biogenesis. Subsequent work, highlighted the role of mitoFAS as a nutrient-sensitive pathway that provides an elegant mechanism whereby acetyl-CoA regulates its own consumption via coordination of lipoic acid synthesis and tricarboxylic acid (TCA) cycle activity, iron-sulfur (FeS) cluster biogenesis, assembly of oxidative phosphorylation complexes, and mitochondrial translation. https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1553890994315-1XIGVQG4TVFQRPK3NBQQ/41467_2018_4564_Fig3_HTML.jpg Functionalizing the Mitochondrial Proteome - Mitochondrial Protein Quality Control Msp1/ATAD1 is a AAA-ATPase protein that we found to reside on the mitochondrial outer membrane. Through a combination of genetics and biochemistry, we showed that it extracts proteins that mis-localize to the mitochondrial outer membrane, which we observed as a surprisingly common phenomenon. We demonstrated this function for the protein family in yeast, human cells, and knockout mice. We found that Vms1 is required for the stress-responsive mitochondrial recruitment of Cdc48/VCP/p97 and Npl4, which play a role in protein extraction and degradation. Further studies led to the conclusion that Vms1 is a critical component of a previously unknown system for mitochondrial protein quality control, eliminating damaged or misfolded proteins that promote progressive mitochondrial dysfunction. https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1553891158993-O412CKMX0CUPVN3LYSOF/nihms600712f1.jpg Functionalizing the Mitochondrial Proteome - Regulation of Electron Transport Chain Assembly We found that both Sdh5 and Sdh8 are required for the assembly of the succinate dehydrogenase complex (Complex II) of the electron transport chain. As a result of these mechanistic functional studies, we were able to discover that familial mutations in human SDH5 (SDHAF2) cause a paraganglioma tumor syndrome. We also discovered a role for Rcf1 in the normal assembly of respiratory supercomplexes in yeast and mammals. Deletion of the RCF1 gene caused impaired respiration and elevated mitochondrial oxidative stress and damage. http://rutter.biochem.utah.edu/research-overview daily 0.75 2024-11-25 http://rutter.biochem.utah.edu/mitomonday daily 0.75 2021-12-14 http://rutter.biochem.utah.edu/contact-us daily 0.75 2025-05-28 https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/1557961831512-XZ10R6IN92SZ98N7KK4U/IMG_20170415_101702.jpg Contact Us - Why Utah? http://rutter.biochem.utah.edu/lab-members daily 0.75 2026-04-19 https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/3385c8f4-692a-4b1f-bacd-73a3bfb34383/Ali+Bouck+10-17-2024+p-1.jpg Lab Members https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/829147d9-68ff-433d-8227-32bbe61789b7/James+Carrington_08-25-2022_img-1.jpg Lab Members https://images.squarespace-cdn.com/content/v1/5beb52c85417fc8adf92d448/90db3931-3b5e-450c-8e10-e3907ee7b3f7/Aaron+Leifer+11-15-2023+p-1.jpg Lab Members 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