Polyamines and eIF5A Hypusination Modulate Mitochondrial Respiration and Macrophage Activation
How cells adapt metabolism to meet demands is an active area of interest across biology. Among a broad range of functions, the polyamine spermidine is needed to hypusinate the translation factor eukaryotic initiation factor 5A (eIF5A). We show here that hypusinated eIF5A (eIF5AH) promotes the effici...
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| Published in | Cell metabolism Vol. 30; no. 2; pp. 352 - 363.e8 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
06.08.2019
Cell Press |
| Subjects | |
| Online Access | Get full text |
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| Abstract | How cells adapt metabolism to meet demands is an active area of interest across biology. Among a broad range of functions, the polyamine spermidine is needed to hypusinate the translation factor eukaryotic initiation factor 5A (eIF5A). We show here that hypusinated eIF5A (eIF5AH) promotes the efficient expression of a subset of mitochondrial proteins involved in the TCA cycle and oxidative phosphorylation (OXPHOS). Several of these proteins have mitochondrial targeting sequences (MTSs) that in part confer an increased dependency on eIF5AH. In macrophages, metabolic switching between OXPHOS and glycolysis supports divergent functional fates stimulated by activation signals. In these cells, hypusination of eIF5A appears to be dynamically regulated after activation. Using in vivo and in vitro models, we show that acute inhibition of this pathway blunts OXPHOS-dependent alternative activation, while leaving aerobic glycolysis-dependent classical activation intact. These results might have implications for therapeutically controlling macrophage activation by targeting the polyamine-eIF5A-hypusine axis.
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•The polyamine synthesis pathway and hypusinated eIF5A modulate mitochondrial OXPHOS•Hypusinated eIF5A maintains TCA cycle and ETC integrity in macrophages•Some mitochondrial enzymes depend on eIF5AH for efficient expression•Inhibition of hypusinated eIF5A blunts macrophage alternative activation
Puleston et al. show that polyamine biosynthesis modulates mitochondrial metabolism through eIF5A hypusination (eIF5AH). They find that inhibiting the polyamine-eIF5A-hypusine pathway blocks OXPHOS-dependent macrophage alternative activation, while leaving aerobic glycolysis-dependent macrophage classical activation intact. These results might have implications for therapeutically controlling macrophage activation by targeting the polyamine-eIF5A-hypusine axis. |
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| AbstractList | How cells adapt metabolism to meet demands is an active area of interest across biology. Among a broad range of functions, the polyamine spermidine is needed to hypusinate the translation factor eukaryotic initiation factor 5A (eIF5A). We show here that hypusinated eIF5A (eIF5AH) promotes the efficient expression of a subset of mitochondrial proteins involved in the TCA cycle and oxidative phosphorylation (OXPHOS). Several of these proteins have mitochondrial targeting sequences (MTSs) that in part confer an increased dependency on eIF5AH. In macrophages, metabolic switching between OXPHOS and glycolysis supports divergent functional fates stimulated by activation signals. In these cells, hypusination of eIF5A appears to be dynamically regulated after activation. Using in vivo and in vitro models, we show that acute inhibition of this pathway blunts OXPHOS-dependent alternative activation, while leaving aerobic glycolysis-dependent classical activation intact. These results might have implications for therapeutically controlling macrophage activation by targeting the polyamine-eIF5A-hypusine axis.
[Display omitted]
•The polyamine synthesis pathway and hypusinated eIF5A modulate mitochondrial OXPHOS•Hypusinated eIF5A maintains TCA cycle and ETC integrity in macrophages•Some mitochondrial enzymes depend on eIF5AH for efficient expression•Inhibition of hypusinated eIF5A blunts macrophage alternative activation
Puleston et al. show that polyamine biosynthesis modulates mitochondrial metabolism through eIF5A hypusination (eIF5AH). They find that inhibiting the polyamine-eIF5A-hypusine pathway blocks OXPHOS-dependent macrophage alternative activation, while leaving aerobic glycolysis-dependent macrophage classical activation intact. These results might have implications for therapeutically controlling macrophage activation by targeting the polyamine-eIF5A-hypusine axis. How cells adapt metabolism to meet demands is an active area of interest across biology. Among a broad range of functions, the polyamine spermidine is needed to hypusinate the translation factor eukaryotic initiation factor 5A (eIF5A). We show here that hypusinated eIF5A (eIF5A ) promotes the efficient expression of a subset of mitochondrial proteins involved in the TCA cycle and oxidative phosphorylation (OXPHOS). Several of these proteins have mitochondrial targeting sequences (MTSs) that in part confer an increased dependency on eIF5AH. In macrophages, metabolic switching between OXPHOS and glycolysis supports divergent functional fates stimulated by activation signals. In these cells, hypusination of eIF5A appears to be dynamically regulated after activation. Using in vivo and in vitro models, we show that acute inhibition of this pathway blunts OXPHOS-dependent alternative activation, while leaving aerobic glycolysis-dependent classical activation intact. These results might have implications for therapeutically controlling macrophage activation by targeting the polyamine-eIF5A-hypusine axis. How cells adapt metabolism to meet demands is an active area of interest across biology. Among a broad range of functions, the polyamine spermidine is needed to hypusinate the translation factor eukaryotic initiation factor 5A (eIF5A). We show here that hypusinated eIF5A (eIF5A H ) promotes the efficient expression of a subset of mitochondrial proteins involved in the TCA cycle and oxidative phosphorylation (OXPHOS). Several of these proteins have mitochondrial targeting sequences (MTSs) that in part confer an increased dependency on eIF5AH. In macrophages, metabolic switching between OXPHOS and glycolysis supports divergent functional fates stimulated by activation signals. In these cells, hypusination of eIF5A appears to be dynamically regulated after activation. Using in vivo and in vitro models, we show that acute inhibition of this pathway blunts OXPHOS-dependent alternative activation, while leaving aerobic glycolysis-dependent classical activation intact. These results might have implications for therapeutically controlling macrophage activation by targeting the polyamine-eIF5A-hypusine axis. • The polyamine synthesis pathway and hypusinated eIF5A modulate mitochondrial OXPHOS • Hypusinated eIF5A maintains TCA cycle and ETC integrity in macrophages • Some mitochondrial enzymes depend on eIF5A H for efficient expression • Inhibition of hypusinated eIF5A blunts macrophage alternative activation Puleston et al. show that polyamine biosynthesis modulates mitochondrial metabolism through eIF5A hypusination (eIF5A H ). They find that inhibiting the polyamine-eIF5A-hypusine pathway blocks OXPHOS-dependent macrophage alternative activation, while leaving aerobic glycolysis-dependent macrophage classical activation intact. These results might have implications for therapeutically controlling macrophage activation by targeting the polyamine-eIF5A-hypusine axis. How cells adapt metabolism to meet demands is an active area of interest across biology. Among a broad range of functions, the polyamine spermidine is needed to hypusinate the translation factor eukaryotic initiation factor 5A (eIF5A). We show here that hypusinated eIF5A (eIF5AH) promotes the efficient expression of a subset of mitochondrial proteins involved in the TCA cycle and oxidative phosphorylation (OXPHOS). Several of these proteins have mitochondrial targeting sequences (MTSs) that in part confer an increased dependency on eIF5AH. In macrophages, metabolic switching between OXPHOS and glycolysis supports divergent functional fates stimulated by activation signals. In these cells, hypusination of eIF5A appears to be dynamically regulated after activation. Using in vivo and in vitro models, we show that acute inhibition of this pathway blunts OXPHOS-dependent alternative activation, while leaving aerobic glycolysis-dependent classical activation intact. These results might have implications for therapeutically controlling macrophage activation by targeting the polyamine-eIF5A-hypusine axis.How cells adapt metabolism to meet demands is an active area of interest across biology. Among a broad range of functions, the polyamine spermidine is needed to hypusinate the translation factor eukaryotic initiation factor 5A (eIF5A). We show here that hypusinated eIF5A (eIF5AH) promotes the efficient expression of a subset of mitochondrial proteins involved in the TCA cycle and oxidative phosphorylation (OXPHOS). Several of these proteins have mitochondrial targeting sequences (MTSs) that in part confer an increased dependency on eIF5AH. In macrophages, metabolic switching between OXPHOS and glycolysis supports divergent functional fates stimulated by activation signals. In these cells, hypusination of eIF5A appears to be dynamically regulated after activation. Using in vivo and in vitro models, we show that acute inhibition of this pathway blunts OXPHOS-dependent alternative activation, while leaving aerobic glycolysis-dependent classical activation intact. These results might have implications for therapeutically controlling macrophage activation by targeting the polyamine-eIF5A-hypusine axis. |
| Author | Paz, Katelyn Austin, S. Kyle Patterson, Annette E. Zehn, Dietmar Sanin, David E. Pällman, Nora Musa, Yaarub Pearce, Erika L. O’Sullivan, David Alfei, Francesca Matsushita, Mai Rospert, Sabine Klein Geltink, Ramon I. Mittler, Gerhard Balabanov, Stefan Pearce, Edward J. Curtis, Jonathan D. Maccari, Maria Elena Buescher, Joerg M. Buck, Michael D. Baixauli, Francesc Field, Cameron S. Caputa, George Kyle, Ryan L. Blazar, Bruce R. Kelly, Beth Castoldi, Angela Cameron, Alanna M. Corrado, Mauro Villa, Matteo Grzes, Katarzyna M. Kabat, Agnieszka M. Zhang, Ying Flachsmann, Lea J. Scherer, Stefanie Puleston, Daniel J. Qiu, Jing |
| AuthorAffiliation | 5 Division of Haematology, University Hospital Zurich and University of Zurich, Zurich 8091, Switzerland 8 Faculty of Biology, University of Freiburg, Freiburg 79104, Germany 7 Institute for Immunodeficiency, Center for Chronic Immunodeficiency, Center for Pediatrics, and Faculty of Medicine, Medical Center - University of Freiburg, Freiburg 79106, Germany 2 The Kennedy Institute of Rheumatology, University of Oxford, Oxford OX3 7FY, UK 3 Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, and BIOSS Centre for Biological Signaling Studies, University of Freiburg, Freiburg 79104, Germany 4 Department of Animal Physiology and Immunology, Technical University of Munich, Freising, Germany 6 Department of Pediatrics, Division of Blood and Marrow Transplantation, University of Minnesota, Minneapolis, MN, USA 1 Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany |
| AuthorAffiliation_xml | – name: 8 Faculty of Biology, University of Freiburg, Freiburg 79104, Germany – name: 3 Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, and BIOSS Centre for Biological Signaling Studies, University of Freiburg, Freiburg 79104, Germany – name: 7 Institute for Immunodeficiency, Center for Chronic Immunodeficiency, Center for Pediatrics, and Faculty of Medicine, Medical Center - University of Freiburg, Freiburg 79106, Germany – name: 4 Department of Animal Physiology and Immunology, Technical University of Munich, Freising, Germany – name: 6 Department of Pediatrics, Division of Blood and Marrow Transplantation, University of Minnesota, Minneapolis, MN, USA – name: 5 Division of Haematology, University Hospital Zurich and University of Zurich, Zurich 8091, Switzerland – name: 1 Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – name: 2 The Kennedy Institute of Rheumatology, University of Oxford, Oxford OX3 7FY, UK |
| Author_xml | – sequence: 1 givenname: Daniel J. surname: Puleston fullname: Puleston, Daniel J. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 2 givenname: Michael D. surname: Buck fullname: Buck, Michael D. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 3 givenname: Ramon I. surname: Klein Geltink fullname: Klein Geltink, Ramon I. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 4 givenname: Ryan L. surname: Kyle fullname: Kyle, Ryan L. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 5 givenname: George surname: Caputa fullname: Caputa, George organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 6 givenname: David surname: O’Sullivan fullname: O’Sullivan, David organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 7 givenname: Alanna M. surname: Cameron fullname: Cameron, Alanna M. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 8 givenname: Angela surname: Castoldi fullname: Castoldi, Angela organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 9 givenname: Yaarub surname: Musa fullname: Musa, Yaarub organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 10 givenname: Agnieszka M. surname: Kabat fullname: Kabat, Agnieszka M. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 11 givenname: Ying surname: Zhang fullname: Zhang, Ying organization: Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, and BIOSS Centre for Biological Signaling Studies, University of Freiburg, Freiburg 79104, Germany – sequence: 12 givenname: Lea J. surname: Flachsmann fullname: Flachsmann, Lea J. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 13 givenname: Cameron S. surname: Field fullname: Field, Cameron S. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 14 givenname: Annette E. surname: Patterson fullname: Patterson, Annette E. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 15 givenname: Stefanie surname: Scherer fullname: Scherer, Stefanie organization: Department of Animal Physiology and Immunology, Technical University of Munich, Freising, Germany – sequence: 16 givenname: Francesca surname: Alfei fullname: Alfei, Francesca organization: Department of Animal Physiology and Immunology, Technical University of Munich, Freising, Germany – sequence: 17 givenname: Francesc surname: Baixauli fullname: Baixauli, Francesc organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 18 givenname: S. Kyle surname: Austin fullname: Austin, S. Kyle organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 19 givenname: Beth surname: Kelly fullname: Kelly, Beth organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 20 givenname: Mai surname: Matsushita fullname: Matsushita, Mai organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 21 givenname: Jonathan D. surname: Curtis fullname: Curtis, Jonathan D. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 22 givenname: Katarzyna M. surname: Grzes fullname: Grzes, Katarzyna M. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 23 givenname: Matteo surname: Villa fullname: Villa, Matteo organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 24 givenname: Mauro surname: Corrado fullname: Corrado, Mauro organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 25 givenname: David E. surname: Sanin fullname: Sanin, David E. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 26 givenname: Jing surname: Qiu fullname: Qiu, Jing organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 27 givenname: Nora surname: Pällman fullname: Pällman, Nora organization: Division of Haematology, University Hospital Zurich and University of Zurich, Zurich 8091, Switzerland – sequence: 28 givenname: Katelyn surname: Paz fullname: Paz, Katelyn organization: Department of Pediatrics, Division of Blood and Marrow Transplantation, University of Minnesota, Minneapolis, MN, USA – sequence: 29 givenname: Maria Elena surname: Maccari fullname: Maccari, Maria Elena organization: Institute for Immunodeficiency, Center for Chronic Immunodeficiency, Center for Pediatrics, and Faculty of Medicine, Medical Center - University of Freiburg, Freiburg 79106, Germany – sequence: 30 givenname: Bruce R. surname: Blazar fullname: Blazar, Bruce R. organization: Department of Pediatrics, Division of Blood and Marrow Transplantation, University of Minnesota, Minneapolis, MN, USA – sequence: 31 givenname: Gerhard surname: Mittler fullname: Mittler, Gerhard organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 32 givenname: Joerg M. surname: Buescher fullname: Buescher, Joerg M. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 33 givenname: Dietmar surname: Zehn fullname: Zehn, Dietmar organization: Department of Animal Physiology and Immunology, Technical University of Munich, Freising, Germany – sequence: 34 givenname: Sabine surname: Rospert fullname: Rospert, Sabine organization: Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, and BIOSS Centre for Biological Signaling Studies, University of Freiburg, Freiburg 79104, Germany – sequence: 35 givenname: Edward J. surname: Pearce fullname: Pearce, Edward J. organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany – sequence: 36 givenname: Stefan surname: Balabanov fullname: Balabanov, Stefan organization: Division of Haematology, University Hospital Zurich and University of Zurich, Zurich 8091, Switzerland – sequence: 37 givenname: Erika L. surname: Pearce fullname: Pearce, Erika L. email: pearce@ie-freiburg.mpg.de organization: Max Planck Institute of Immunobiology and Epigenetics, Freiburg 79108, Germany |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31130465$$D View this record in MEDLINE/PubMed |
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| Keywords | hypusination immunometabolism deoxyhypusine hydroxylase metabolism macrophage activation deoxyhypusine synthase polyamines eIF5A |
| Language | English |
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| Title | Polyamines and eIF5A Hypusination Modulate Mitochondrial Respiration and Macrophage Activation |
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