ACAD10 and ACAD11 allow entry of 4-hydroxy fatty acids into β-oxidation.
4-hydroxy fatty acids
ACAD10
ACAD11
Beta-oxidation
Haloacid dehalogenase domain
Phosphohydroxyacyl-CoA
Journal
Cellular and molecular life sciences : CMLS
ISSN: 1420-9071
Titre abrégé: Cell Mol Life Sci
Pays: Switzerland
ID NLM: 9705402
Informations de publication
Date de publication:
22 Aug 2024
22 Aug 2024
Historique:
received:
27
04
2024
accepted:
05
08
2024
revised:
02
08
2024
medline:
23
8
2024
pubmed:
23
8
2024
entrez:
22
8
2024
Statut:
epublish
Résumé
Hydroxylated fatty acids are important intermediates in lipid metabolism and signaling. Surprisingly, the metabolism of 4-hydroxy fatty acids remains largely unexplored. We found that both ACAD10 and ACAD11 unite two enzymatic activities to introduce these metabolites into mitochondrial and peroxisomal β-oxidation, respectively. First, they phosphorylate 4-hydroxyacyl-CoAs via a kinase domain, followed by an elimination of the phosphate to form enoyl-CoAs catalyzed by an acyl-CoA dehydrogenase (ACAD) domain. Studies in knockout cell lines revealed that ACAD10 preferentially metabolizes shorter chain 4-hydroxy fatty acids than ACAD11 (i.e. 6 carbons versus 10 carbons). Yet, recombinant proteins showed comparable activity on the corresponding 4-hydroxyacyl-CoAs. This suggests that the localization of ACAD10 and ACAD11 to mitochondria and peroxisomes, respectively, might influence their physiological substrate spectrum. Interestingly, we observed that ACAD10 is cleaved internally during its maturation generating a C-terminal part consisting of the ACAD domain, and an N-terminal part comprising the kinase domain and a haloacid dehalogenase (HAD) domain. HAD domains often exhibit phosphatase activity, but negligible activity was observed in the case of ACAD10. Yet, inactivation of a presumptive key residue in this domain significantly increased the kinase activity, suggesting that this domain might have acquired a regulatory function to prevent accumulation of the phospho-hydroxyacyl-CoA intermediate. Taken together, our work reveals that 4-hydroxy fatty acids enter mitochondrial and peroxisomal fatty acid β-oxidation via two enzymes with an overlapping substrate repertoire.
Identifiants
pubmed: 39174697
doi: 10.1007/s00018-024-05397-8
pii: 10.1007/s00018-024-05397-8
doi:
Substances chimiques
Fatty Acids
0
Acyl-CoA Dehydrogenases
EC 1.3.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
367Subventions
Organisme : European Research Council
ID : 771704
Pays : International
Organisme : Fonds De La Recherche Scientifique - FNRS
ID : WELBIO
Organisme : Fonds De La Recherche Scientifique - FNRS
ID : PDR
Organisme : Fonds De La Recherche Scientifique - FNRS
ID : CDR
Organisme : Fonds De La Recherche Scientifique - FNRS
ID : EQP
Organisme : Fonds De La Recherche Scientifique - FNRS
ID : WELBIO
Organisme : Fondation Médicale Reine Elisabeth
ID : Prix Vicomtesse Valine de Spoelberch
Informations de copyright
© 2024. The Author(s).
Références
Christie WW, Harwood JL (2020) Oxidation of polyunsaturated fatty acids to produce lipid mediators. Essays Biochem 64(3):401–421. https://doi.org/10.1042/EBC20190082
doi: 10.1042/EBC20190082
pubmed: 32618335
pmcid: 7517362
Kahnt AS, Schebb NH, Steinhilber D (2023) Formation of lipoxins and resolvins in human leukocytes. Prostaglandins Other Lipid Mediat 166:106726. https://doi.org/10.1016/j.prostaglandins.2023.106726
doi: 10.1016/j.prostaglandins.2023.106726
pubmed: 36878381
Vidar Hansen T, Serhan CN (2022) Protectins: their biosynthesis, metabolism and structure-functions. Biochem Pharmacol 206:115330. https://doi.org/10.1016/j.bcp.2022.115330
doi: 10.1016/j.bcp.2022.115330
pubmed: 36341938
Shen HC, Hammock BD (2012) Discovery of inhibitors of soluble epoxide hydrolase: a target with multiple potential therapeutic indications. J Med Chem 55(5):1789–1808. https://doi.org/10.1021/jm201468j
doi: 10.1021/jm201468j
pubmed: 22168898
pmcid: 3420824
Piotto S, Trapani A, Bianchino E, Ibarguren M, Lopez DJ, Busquets X, Concilio S (2014) The effect of hydroxylated fatty acid-containing phospholipids in the remodeling of lipid membranes. Biochem Biophys Acta 1838(6):1509–1517. https://doi.org/10.1016/j.bbamem.2014.01.014
doi: 10.1016/j.bbamem.2014.01.014
pubmed: 24463068
Carroll J, Fearnley IM, Shannon RJ, Hirst J, Walker JE (2003) Analysis of the subunit composition of complex I from bovine heart mitochondria. Mol Cell Proteom 2(2):117–126. https://doi.org/10.1074/mcp.M300014-MCP200
doi: 10.1074/mcp.M300014-MCP200
Ayala A, Munoz MF, Arguelles S (2014) Lipid peroxidation: production, metabolism, and signaling mechanisms of malondialdehyde and 4-hydroxy-2-nonenal. Oxid Med Cell Longev 2014:360438. https://doi.org/10.1155/2014/360438
doi: 10.1155/2014/360438
pubmed: 24999379
pmcid: 4066722
Zhang GF, Kombu RS, Kasumov T, Han Y, Sadhukhan S, Zhang J, Sayre LM, Ray D, Gibson KM, Anderson VA, Tochtrop GP, Brunengraber H (2009) Catabolism of 4-hydroxyacids and 4-hydroxynonenal via 4-hydroxy-4-phosphoacyl-CoAs. J Biol Chem 284(48):33521–33534. https://doi.org/10.1074/jbc.M109.055665
doi: 10.1074/jbc.M109.055665
pubmed: 19759021
pmcid: 2785196
Sanchez-Alvarez A, Ruiz-Lopez N, Moreno-Perez AJ, Venegas-Caleron M, Martinez-Force E, Garces R, Salas JJ (2022) Metabolism and accumulation of hydroxylated fatty acids by castor (Ricinus comunis) seed microsomes. Plant Physiol Biochem 170:266–274. https://doi.org/10.1016/j.plaphy.2021.12.010
doi: 10.1016/j.plaphy.2021.12.010
pubmed: 34929430
Saeki R, Yoshinaga K, Tago A, Tanaka S, Yoshinaga-Kiriake A, Nagai T, Yoshida A, Gotoh N (2022) Quantitative analysis of lactone enantiomers in butter and margarine through the combination of solvent extraction and enantioselective gas chromatography–mass spectrometry. J Agric Food Chem 70(18):5756–5763. https://doi.org/10.1021/acs.jafc.2c01480
doi: 10.1021/acs.jafc.2c01480
pubmed: 35482605
Miyamoto J, Mizukure T, Park SB, Kishino S, Kimura I, Hirano K, Bergamo P, Rossi M, Suzuki T, Arita M, Ogawa J, Tanabe S (2015) A gut microbial metabolite of linoleic acid, 10-hydroxy-cis-12-octadecenoic acid, ameliorates intestinal epithelial barrier impairment partially via GPR40-MEK-ERK pathway. J Biol Chem 290(5):2902–2918. https://doi.org/10.1074/jbc.M114.610733
doi: 10.1074/jbc.M114.610733
pubmed: 25505251
Tunaru S, Althoff TF, Nusing RM, Diener M, Offermanns S (2012) Castor oil induces laxation and uterus contraction via ricinoleic acid activating prostaglandin EP3 receptors. Proc Natl Acad Sci USA 109(23):9179–9184. https://doi.org/10.1073/pnas.1201627109
doi: 10.1073/pnas.1201627109
pubmed: 22615395
pmcid: 3384204
Wanders RJ, Komen J, Kemp S (2011) Fatty acid omega-oxidation as a rescue pathway for fatty acid oxidation disorders in humans. FEBS J 278(2):182–194. https://doi.org/10.1111/j.1742-4658.2010.07947.x
doi: 10.1111/j.1742-4658.2010.07947.x
pubmed: 21156023
Jansen GA, Wanders RJ (2006) Alpha-oxidation. Biochem Biophys Acta 1763(12):1403–1412. https://doi.org/10.1016/j.bbamcr.2006.07.012
doi: 10.1016/j.bbamcr.2006.07.012
pubmed: 16934890
Harris SR, Zhang GF, Sadhukhan S, Murphy AM, Tomcik KA, Vazquez EJ, Anderson VE, Tochtrop GP, Brunengraber H (2011) Metabolism of levulinate in perfused rat livers and live rats: conversion to the drug of abuse 4-hydroxypentanoate. J Biol Chem 286(7):5895–5904. https://doi.org/10.1074/jbc.M110.196808
doi: 10.1074/jbc.M110.196808
pubmed: 21126961
Li Q, Tomcik K, Zhang S, Puchowicz MA, Zhang GF (2012) Dietary regulation of catabolic disposal of 4-hydroxynonenal analogs in rat liver. Free Radic Biol Med 52(6):1043–1053. https://doi.org/10.1016/j.freeradbiomed.2011.12.022
doi: 10.1016/j.freeradbiomed.2011.12.022
pubmed: 22245097
pmcid: 3289253
Sadhukhan S, Han Y, Zhang GF, Brunengraber H, Tochtrop GP (2010) Using isotopic tools to dissect and quantitate parallel metabolic pathways. J Am Chem Soc 132(18):6309–6311. https://doi.org/10.1021/ja100399m
doi: 10.1021/ja100399m
pubmed: 20408520
Rand JM, Pisithkul T, Clark RL, Thiede JM, Mehrer CR, Agnew DE, Campbell CE, Markley AL, Price MN, Ray J, Wetmore KM, Suh Y, Arkin AP, Deutschbauer AM, Amador-Noguez D, Pfleger BF (2017) A metabolic pathway for catabolizing levulinic acid in bacteria. Nat Microbiol 2(12):1624–1634. https://doi.org/10.1038/s41564-017-0028-z
doi: 10.1038/s41564-017-0028-z
pubmed: 28947739
pmcid: 5705400
Kaul M, Barbieri CM, Srinivasan AR, Pilch DS (2007) Molecular determinants of antibiotic recognition and resistance by aminoglycoside phosphotransferase (3’)-IIIa: a calorimetric and mutational analysis. J Mol Biol 369(1):142–156. https://doi.org/10.1016/j.jmb.2007.02.103
doi: 10.1016/j.jmb.2007.02.103
pubmed: 17418235
pmcid: 2040079
Ghisla S, Thorpe C (2004) Acyl-CoA dehydrogenases. A mechanistic overview. Eur J Biochem 271(3):494–508. https://doi.org/10.1046/j.1432-1033.2003.03946.x
doi: 10.1046/j.1432-1033.2003.03946.x
pubmed: 14728676
Seifried A, Schultz J, Gohla A (2013) Human HAD phosphatases: structure, mechanism, and roles in health and disease. FEBS J 280(2):549–571. https://doi.org/10.1111/j.1742-4658.2012.08633.x
doi: 10.1111/j.1742-4658.2012.08633.x
pubmed: 22607316
Yew MJ, Heywood SE, Ng J, West OM, Pal M, Kueh A, Lancaster GI, Myers S, Yang C, Liu Y, Reibe S, Mellett NA, Meikle PJ, Febbraio MA, Greening DW, Drew BG, Henstridge DC (2024) ACAD10 is not required for metformin’s metabolic actions or for maintenance of whole-body metabolism in C57BL/6J mice. Diabetes Obes Metab 26(5):1731–1745. https://doi.org/10.1111/dom.15484
doi: 10.1111/dom.15484
pubmed: 38351663
Wu L, Zhou B, Oshiro-Rapley N, Li M, Paulo JA, Webster CM, Mou F, Kacergis MC, Talkowski ME, Carr CE, Gygi SP, Zheng B, Soukas AA (2016) An ancient, unified mechanism for metformin growth inhibition in C. elegans and cancer. Cell 167(7):1705–1718. https://doi.org/10.1016/j.cell.2016.11.055
doi: 10.1016/j.cell.2016.11.055
pubmed: 27984722
pmcid: 5390486
Schmidt O, Pfanner N, Meisinger C (2010) Mitochondrial protein import: from proteomics to functional mechanisms. Nat Rev Mol Cell Biol 11(9):655–667. https://doi.org/10.1038/nrm2959
doi: 10.1038/nrm2959
pubmed: 20729931
Redl I, Fisicaro C, Dutton O, Hoffmann F, Henderson L, Owens BMJ, Heberling M, Paci E, Tamiola K (2023) ADOPT: intrinsic protein disorder prediction through deep bidirectional transformers. NAR Genom Bioinform 5(2):lqad041. https://doi.org/10.1093/nargab/lqad041
doi: 10.1093/nargab/lqad041
pubmed: 37138579
pmcid: 10150328
El Rayes J, Szewczyk J, Deghelt M, Csoma N, Matagne A, Iorga BI, Cho SH, Collet JF (2021) Disorder is a critical component of lipoprotein sorting in gram-negative bacteria. Nat Chem Biol 17(10):1093–1100. https://doi.org/10.1038/s41589-021-00845-z
doi: 10.1038/s41589-021-00845-z
pubmed: 34326538
Mossmann D, Meisinger C, Vogtle FN (2012) Processing of mitochondrial presequences. Biochem Biophys Acta 1819(9–10):1098–1106. https://doi.org/10.1016/j.bbagrm.2011.11.007
doi: 10.1016/j.bbagrm.2011.11.007
pubmed: 22172993
Almagro Armenteros JJ, Salvatore M, Emanuelsson O, Winther O, von Heijne G, Elofsson A, Nielsen H (2019) Detecting sequence signals in targeting peptides using deep learning. Life Sci Alliance. https://doi.org/10.26508/lsa.201900429
doi: 10.26508/lsa.201900429
pubmed: 31570514
pmcid: 6769257
Fukasawa Y, Tsuji J, Fu SC, Tomii K, Horton P, Imai K (2015) MitoFates: improved prediction of mitochondrial targeting sequences and their cleavage sites. Mol Cell Proteom 14(4):1113–1126. https://doi.org/10.1074/mcp.M114.043083
doi: 10.1074/mcp.M114.043083
Taylor AB, Smith BS, Kitada S, Kojima K, Miyaura H, Otwinowski Z, Ito A, Deisenhofer J (2001) Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences. Structure 9(7):615–625. https://doi.org/10.1016/s0969-2126(01)00621-9
doi: 10.1016/s0969-2126(01)00621-9
pubmed: 11470436
Friedl J, Knopp MR, Groh C, Paz E, Gould SB, Herrmann JM, Boos F (2020) More than just a ticket canceller: the mitochondrial processing peptidase tailors complex precursor proteins at internal cleavage sites. Mol Biol Cell 31(24):2657–2668. https://doi.org/10.1091/mbc.E20-08-0524
doi: 10.1091/mbc.E20-08-0524
pubmed: 32997570
pmcid: 8734313
Woellhaf MW, Sommer F, Schroda M, Herrmann JM (2016) Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein. Mol Biol Cell 27(20):3031–3039. https://doi.org/10.1091/mbc.E16-07-0513
doi: 10.1091/mbc.E16-07-0513
pubmed: 27582385
pmcid: 5063612
Varadi M, Bertoni D, Magana P, Paramval U, Pidruchna I, Radhakrishnan M, Tsenkov M, Nair S, Mirdita M, Yeo J, Kovalevskiy O, Tunyasuvunakool K, Laydon A, Zidek A, Tomlinson H, Hariharan D, Abrahamson J, Green T, Jumper J, Birney E, Steinegger M, Hassabis D, Velankar S (2024) AlphaFold Protein Structure Database in 2024: providing structure coverage for over 214 million protein sequences. Nucleic Acids Res 52(D1):D368–D375. https://doi.org/10.1093/nar/gkad1011
doi: 10.1093/nar/gkad1011
pubmed: 37933859
Swigonova Z, Mohsen AW, Vockley J (2009) Acyl-CoA dehydrogenases: Dynamic history of protein family evolution. J Mol Evol 69(2):176–193. https://doi.org/10.1007/s00239-009-9263-0
doi: 10.1007/s00239-009-9263-0
pubmed: 19639238
pmcid: 4136416
Parker BL, Calkin AC, Seldin MM, Keating MF, Tarling EJ, Yang P, Moody SC, Liu Y, Zerenturk EJ, Needham EJ, Miller ML, Clifford BL, Morand P, Watt MJ, Meex RCR, Peng KY, Lee R, Jayawardana K, Pan C, Mellett NA, Weir JM, Lazarus R, Lusis AJ, Meikle PJ, James DE, de Aguiar Vallim TQ, Drew BG (2019) An integrative systems genetic analysis of mammalian lipid metabolism. Nature 567(7747):187–193. https://doi.org/10.1038/s41586-019-0984-y
doi: 10.1038/s41586-019-0984-y
pubmed: 30814737
pmcid: 6656374
Camoes F, Islinger M, Guimaraes SC, Kilaru S, Schuster M, Godinho LF, Steinberg G, Schrader M (2015) New insights into the peroxisomal protein inventory: Acyl-CoA oxidases and -dehydrogenases are an ancient feature of peroxisomes. Biochem Biophys Acta 1853(1):111–125. https://doi.org/10.1016/j.bbamcr.2014.10.005
doi: 10.1016/j.bbamcr.2014.10.005
pubmed: 25307522
Wiese S, Gronemeyer T, Ofman R, Kunze M, Grou CP, Almeida JA, Eisenacher M, Stephan C, Hayen H, Schollenberger L, Korosec T, Waterham HR, Schliebs W, Erdmann R, Berger J, Meyer HE, Just W, Azevedo JE, Wanders RJ, Warscheid B (2007) Proteomics characterization of mouse kidney peroxisomes by tandem mass spectrometry and protein correlation profiling. Mol Cell Proteom 6(12):2045–2057. https://doi.org/10.1074/mcp.M700169-MCP200
doi: 10.1074/mcp.M700169-MCP200
Islinger M, Luers GH, Li KW, Loos M, Volkl A (2007) Rat liver peroxisomes after fibrate treatment. A survey using quantitative mass spectrometry. J Biol Chem 282(32):23055–23069. https://doi.org/10.1074/jbc.M610910200
doi: 10.1074/jbc.M610910200
pubmed: 17522052
Chornyi S, Koster J, Li J, Waterham HR (2024) Studying the topology of peroxisomal acyl-CoA synthetases using self-assembling split sfGFP. Histochem Cell Biol 161(2):133–144. https://doi.org/10.1007/s00418-023-02257-7
doi: 10.1007/s00418-023-02257-7
pubmed: 38243092
pmcid: 10822792
Watkins PA, Ellis JM (2012) Peroxisomal acyl-CoA synthetases. Biochem Biophys Acta 1822(9):1411–1420. https://doi.org/10.1016/j.bbadis.2012.02.010
doi: 10.1016/j.bbadis.2012.02.010
pubmed: 22366061
Rashan EH, Bartlett AK, Khana DB, Zhang J, Jain R, Smith AJ, Baker ZN, Cook T, Caldwell A, Chevalier AR, Pfleger BF, Yuan P, Amador-Noguez D, Simcox JA, Pagliarini DJ (2024) ACAD10 and ACAD11 enable mammalian 4-hydroxy acid lipid catabolism. bioRxiv. https://doi.org/10.1101/2024.01.09.574893
doi: 10.1101/2024.01.09.574893
pubmed: 38260250
pmcid: 10802472
Pedley AM, Pareek V, Benkovic SJ (2022) The purinosome: a case study for a mammalian metabolon. Annu Rev Biochem 91:89–106. https://doi.org/10.1146/annurev-biochem-032620-105728
doi: 10.1146/annurev-biochem-032620-105728
pubmed: 35320684
pmcid: 9531488
Leibundgut M, Maier T, Jenni S, Ban N (2008) The multienzyme architecture of eukaryotic fatty acid synthases. Curr Opin Struct Biol 18(6):714–725. https://doi.org/10.1016/j.sbi.2008.09.008
doi: 10.1016/j.sbi.2008.09.008
pubmed: 18948193
Pareek V, Sha Z, He J, Wingreen NS, Benkovic SJ (2021) Metabolic channeling: predictions, deductions, and evidence. Mol Cell 81(18):3775–3785. https://doi.org/10.1016/j.molcel.2021.08.030
doi: 10.1016/j.molcel.2021.08.030
pubmed: 34547238
pmcid: 8485759
He M, Pei Z, Mohsen AW, Watkins P, Murdoch G, Van Veldhoven PP, Ensenauer R, Vockley J (2011) Identification and characterization of new long chain acyl-CoA dehydrogenases. Mol Genet Metab 102(4):418–429. https://doi.org/10.1016/j.ymgme.2010.12.005
doi: 10.1016/j.ymgme.2010.12.005
pubmed: 21237683
Collet JF, Stroobant V, Pirard M, Delpierre G, Van Schaftingen E (1998) A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif. J Biol Chem 273(23):14107–14112. https://doi.org/10.1074/jbc.273.23.14107
doi: 10.1074/jbc.273.23.14107
pubmed: 9603909
Chang A, Jeske L, Ulbrich S, Hofmann J, Koblitz J, Schomburg I, Neumann-Schaal M, Jahn D, Schomburg D (2021) BRENDA, the ELIXIR core data resource in 2021: new developments and updates. Nucleic Acids Res 49(D1):D498–D508. https://doi.org/10.1093/nar/gkaa1025
doi: 10.1093/nar/gkaa1025
pubmed: 33211880
Kitzing K, Auweter S, Amrhein N, Macheroux P (2004) Mechanism of chorismate synthase. Role of the two invariant histidine residues in the active site. J Biol Chem 279(10):9451–9461. https://doi.org/10.1074/jbc.M312471200
doi: 10.1074/jbc.M312471200
pubmed: 14668332
Hubbard PA, Liang X, Schulz H, Kim JJ (2003) The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase. J Biol Chem 278(39):37553–37560. https://doi.org/10.1074/jbc.M304642200
doi: 10.1074/jbc.M304642200
pubmed: 12840019
Liang X, Thorpe C, Schulz H (2000) 2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-sulfur flavoprotein that functions in fatty acid beta-oxidation. Arch Biochem Biophys 380(2):373–379. https://doi.org/10.1006/abbi.2000.1941
doi: 10.1006/abbi.2000.1941
pubmed: 10933894
Lau SM, Powell P, Buettner H, Ghisla S, Thorpe C (1986) Medium-chain acyl coenzyme A dehydrogenase from pig kidney has intrinsic enoyl coenzyme a hydratase activity. Biochemistry 25(15):4184–4189. https://doi.org/10.1021/bi00363a003
doi: 10.1021/bi00363a003
pubmed: 3756134
Gao XR, Chiariglione M, Arch AJ (2022) Whole-exome sequencing study identifies rare variants and genes associated with intraocular pressure and glaucoma. Nat Commun 13(1):7376. https://doi.org/10.1038/s41467-022-35188-3
doi: 10.1038/s41467-022-35188-3
pubmed: 36450729
pmcid: 9712679
Cho SB, Jang J (2021) A genome-wide association study of a Korean population identifies genetic susceptibility to hypertension based on sex-specific differences. Genes (Basel). https://doi.org/10.3390/genes12111804
doi: 10.3390/genes12111804
pubmed: 34946840
pmcid: 9459129
Yamada Y, Sakuma J, Takeuchi I, Yasukochi Y, Kato K, Oguri M, Fujimaki T, Horibe H, Muramatsu M, Sawabe M, Fujiwara Y, Taniguchi Y, Obuchi S, Kawai H, Shinkai S, Mori S, Arai T, Tanaka M (2017) Identification of polymorphisms in 12q24.1, ACAD10, and BRAP as novel genetic determinants of blood pressure in Japanese by exome-wide association studies. Oncotarget 8(26):43068–43079. https://doi.org/10.18632/oncotarget.17474
doi: 10.18632/oncotarget.17474
pubmed: 28562329
pmcid: 5522128
Mittal K, Goncalves VF, Harripaul R, Cuperfain AB, Rollins B, Tiwari AK, Zai CC, Maciukiewicz M, Muller DJ, Vawter MP, Kennedy JL (2017) A comprehensive analysis of mitochondrial genes variants and their association with antipsychotic-induced weight gain. Schizophr Res 187:67–73. https://doi.org/10.1016/j.schres.2017.06.046
doi: 10.1016/j.schres.2017.06.046
pubmed: 28693754
pmcid: 5660917
Bian L, Hanson RL, Muller YL, Ma L, Investigators M, Kobes S, Knowler WC, Bogardus C, Baier LJ (2010) Variants in ACAD10 are associated with type 2 diabetes, insulin resistance and lipid oxidation in Pima Indians. Diabetologia 53(7):1349–1353. https://doi.org/10.1007/s00125-010-1695-y
doi: 10.1007/s00125-010-1695-y
pubmed: 20390405
pmcid: 2947857
Zeng M, Liu Y, Xie Y (2023) Association between ALDH2 polymorphisms and the risk of diabetes mellitus in hypertensive patients. Int J Gen Med 16:5719–5727. https://doi.org/10.2147/IJGM.S435598
doi: 10.2147/IJGM.S435598
pubmed: 38084269
pmcid: 10710740
Chang YC, Lee HL, Yang W, Hsieh ML, Liu CC, Lee TY, Huang JY, Nong JY, Li FA, Chuang HL, Ding ZZ, Su WL, Chueh LY, Tsai YT, Chen CH, Mochly-Rosen D, Chuang LM (2023) A common East-Asian ALDH2 mutation causes metabolic disorders and the therapeutic effect of ALDH2 activators. Nat Commun 14(1):5971. https://doi.org/10.1038/s41467-023-41570-6
doi: 10.1038/s41467-023-41570-6
pubmed: 37749090
pmcid: 10520061
Sakaue S, Kanai M, Tanigawa Y, Karjalainen J, Kurki M, Koshiba S, Narita A, Konuma T, Yamamoto K, Akiyama M, Ishigaki K, Suzuki A, Suzuki K, Obara W, Yamaji K, Takahashi K, Asai S, Takahashi Y, Suzuki T, Shinozaki N, Yamaguchi H, Minami S, Murayama S, Yoshimori K, Nagayama S, Obata D, Higashiyama M, Masumoto A, Koretsune Y, FinnGen IK, Terao C, Yamauchi T, Komuro I, Kadowaki T, Tamiya G, Yamamoto M, Nakamura Y, Kubo M, Murakami Y, Yamamoto K, Kamatani Y, Palotie A, Rivas MA, Daly MJ, Matsuda K, Okada Y (2021) A cross-population atlas of genetic associations for 220 human phenotypes. Nat Genet 53(10):1415–1424. https://doi.org/10.1038/s41588-021-00931-x
doi: 10.1038/s41588-021-00931-x
pubmed: 34594039
Zhu Y, Zhang D, Zhou D, Li Z, Li Z, Fang L, Yang M, Shan Z, Li H, Chen J, Zhou X, Ye W, Yu S, Li H, Cai L, Liu C, Zhang J, Wang L, Lai Y, Ruan L, Sun Z, Zhang S, Wang H, Liu Y, Xu Y, Ling J, Xu C, Zhang Y, Lv D, Yuan Z, Zhang J, Zhang Y, Shi Y, Lai M (2017) Susceptibility loci for metabolic syndrome and metabolic components identified in Han Chinese: a multi-stage genome-wide association study. J Cell Mol Med 21(6):1106–1116. https://doi.org/10.1111/jcmm.13042
doi: 10.1111/jcmm.13042
pubmed: 28371326
pmcid: 5431133
Bloom K, Mohsen AW, Karunanidhi A, El Demellawy D, Reyes-Mugica M, Wang Y, Ghaloul-Gonzalez L, Otsubo C, Tobita K, Muzumdar R, Gong Z, Tas E, Basu S, Chen J, Bennett M, Hoppel C, Vockley J (2018) Investigating the link of ACAD10 deficiency to type 2 diabetes mellitus. J Inherit Metab Dis 41(1):49–57. https://doi.org/10.1007/s10545-017-0013-y
doi: 10.1007/s10545-017-0013-y
pubmed: 28120165
Kirby T, Walters DC, Brown M, Jansen E, Salomons GS, Turgeon C, Rinaldo P, Arning E, Ashcraft P, Bottiglieri T, Roullet JB, Gibson KM (2020) Post-mortem tissue analyses in a patient with succinic semialdehyde dehydrogenase deficiency (SSADHD). I Metabolomic outcomes. Metab Brain Dis 35(4):601–614. https://doi.org/10.1007/s11011-020-00550-1
doi: 10.1007/s11011-020-00550-1
pubmed: 32172518
pmcid: 7180121
Misheva M, Kotzamanis K, Davies LC, Tyrrell VJ, Rodrigues PRS, Benavides GA, Hinz C, Murphy RC, Kennedy P, Taylor PR, Rosas M, Jones SA, McLaren JE, Deshpande S, Andrews R, Schebb NH, Czubala MA, Gurney M, Aldrovandi M, Meckelmann SW, Ghazal P, Darley-Usmar V, White DA, O’Donnell VB (2022) Oxylipin metabolism is controlled by mitochondrial beta-oxidation during bacterial inflammation. Nat Commun 13(1):139. https://doi.org/10.1038/s41467-021-27766-8
doi: 10.1038/s41467-021-27766-8
pubmed: 35013270
pmcid: 8748967
Sanjana NE, Shalem O, Zhang F (2014) Improved vectors and genome-wide libraries for CRISPR screening. Nat Methods 11(8):783–784. https://doi.org/10.1038/nmeth.3047
doi: 10.1038/nmeth.3047
pubmed: 25075903
pmcid: 4486245
Gerin I, Ury B, Breloy I, Bouchet-Seraphin C, Noel G, Bolsee J, Halbout M, Graff J, Vertommen D, Muccioli GG, Seta N, Grahn A, Van Schaftingen E, Bommer GT (2016) ISPD produces CDP-ribitol used by FKTN and FKRP to transfer ribitol-phosphate onto a-dystroglycan. Nat Commun 7:11534. https://doi.org/10.1038/ncomms11534
doi: 10.1038/ncomms11534
pubmed: 27194101
pmcid: 4873967
Gibson DG, Young L, Chuang RY, Venter JC, Hutchison CA 3rd, Smith HO (2009) Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat Methods 6(5):343–345. https://doi.org/10.1038/nmeth.1318
doi: 10.1038/nmeth.1318
pubmed: 19363495
Jordan M, Wurm F (2004) Transfection of adherent and suspended cells by calcium phosphate. Methods 33(2):136–143. https://doi.org/10.1016/j.ymeth.2003.11.011
doi: 10.1016/j.ymeth.2003.11.011
pubmed: 15121168
Heremans IP, Caligiore F, Gerin I, Bury M, Lutz M, Graff J, Stroobant V, Vertommen D, Teleman AA, Van Schaftingen E, Bommer GT (2022) Parkinson’s disease protein PARK7 prevents metabolite and protein damage caused by a glycolytic metabolite. Proc Natl Acad Sci U S A. https://doi.org/10.1073/pnas.2111338119
doi: 10.1073/pnas.2111338119
pubmed: 35385350
pmcid: 9169712
Coulier L, Bas R, Jespersen S, Verheij E, van der Werf MJ, Hankemeier T (2006) Simultaneous quantitative analysis of metabolites using ion-pair liquid chromatography-electrospray ionization mass spectrometry. Anal Chem 78(18):6573–6582. https://doi.org/10.1021/ac0607616
doi: 10.1021/ac0607616
pubmed: 16970336
Gerin I, Noel G, Bolsee J, Haumont O, Van Schaftingen E, Bommer GT (2014) Identification of TP53-induced glycolysis and apoptosis regulator (TIGAR) as the phosphoglycolate-independent 2,3-bisphosphoglycerate phosphatase. Biochem J 458(3):439–448. https://doi.org/10.1042/BJ20130841
doi: 10.1042/BJ20130841
pubmed: 24423178
Kitagawa M, Ara T, Arifuzzaman M, Ioka-Nakamichi T, Inamoto E, Toyonaga H, Mori H (2005) Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res 12(5):291–299. https://doi.org/10.1093/dnares/dsi012
doi: 10.1093/dnares/dsi012
pubmed: 16769691
Šidák Z (1967) Rectangular confidence regions for the means of multivariate normal distributions. J Am Stat Assoc 62(318):626–633. https://doi.org/10.1080/01621459.1967.10482935
doi: 10.1080/01621459.1967.10482935
Dunnett CW (1964) New tables for multiple comparisons with a control. Biometrics 20:482–491. https://doi.org/10.2307/2528490
doi: 10.2307/2528490