PARK7/DJ-1 promotes pyruvate dehydrogenase activity and maintains T
Journal
Nature metabolism
ISSN: 2522-5812
Titre abrégé: Nat Metab
Pays: Germany
ID NLM: 101736592
Informations de publication
Date de publication:
05 2022
05 2022
Historique:
received:
20
12
2019
accepted:
20
04
2022
pubmed:
27
5
2022
medline:
9
6
2022
entrez:
26
5
2022
Statut:
ppublish
Résumé
Pyruvate dehydrogenase (PDH) is the gatekeeper enzyme of the tricarboxylic acid (TCA) cycle. Here we show that the deglycase DJ-1 (encoded by PARK7, a key familial Parkinson's disease gene) is a pacemaker regulating PDH activity in CD4
Identifiants
pubmed: 35618940
doi: 10.1038/s42255-022-00576-y
pii: 10.1038/s42255-022-00576-y
doi:
Substances chimiques
Pyruvates
0
Oxidoreductases
EC 1.-
PARK7 protein, mouse
EC 3.1.2.-
Protein Deglycase DJ-1
EC 3.1.2.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
589-607Informations de copyright
© 2022. The Author(s), under exclusive licence to Springer Nature Limited.
Références
Smeitink, J., van den Heuvel, L. & DiMauro, S. The genetics and pathology of oxidative phosphorylation. Nat. Rev. Genet. 2, 342–352 (2001).
doi: 10.1038/35072063
pubmed: 11331900
O’Neill, L. A., Kishton, R. J. & Rathmell, J. A guide to immunometabolism for immunologists. Nat. Rev. Immunol. 16, 553–565 (2016).
doi: 10.1038/nri.2016.70
pubmed: 27396447
pmcid: 5001910
Abou-Sleiman, P. M., Muqit, M. M. & Wood, N. W. Expanding insights of mitochondrial dysfunction in Parkinson’s disease. Nat. Rev. Neurosci. 7, 207–219 (2006).
doi: 10.1038/nrn1868
pubmed: 16495942
Mizuno, Y. et al. Deficiencies in complex I subunits of the respiratory chain in Parkinson’s disease. Biochem. Biophys. Res. Commun. 163, 1450–1455 (1989).
doi: 10.1016/0006-291X(89)91141-8
pubmed: 2551290
Schapira, A. H. et al. Mitochondrial complex I deficiency in Parkinson’s disease. J. Neurochem. 54, 823–827 (1990).
doi: 10.1111/j.1471-4159.1990.tb02325.x
pubmed: 2154550
González-Rodríguez, P. et al. Disruption of mitochondrial complex I induces progressive parkinsonism. Nature 599, 650–656 (2021).
doi: 10.1038/s41586-021-04059-0
pubmed: 34732887
Bonifati, V. et al. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 299, 256–259 (2003).
doi: 10.1126/science.1077209
pubmed: 12446870
Hayashi, T. et al. DJ-1 binds to mitochondrial complex I and maintains its activity. Biochem. Biophys. Res. Commun. 390, 667–672 (2009).
doi: 10.1016/j.bbrc.2009.10.025
pubmed: 19822128
Irrcher, I. et al. Loss of the Parkinson’s disease-linked gene DJ-1 perturbs mitochondrial dynamics. Hum. Mol. Genet. 19, 3734–3746 (2010).
doi: 10.1093/hmg/ddq288
pubmed: 20639397
Krebiehl, G. et al. Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson’s disease-associated protein DJ-1. PLoS ONE 5, e9367 (2010).
doi: 10.1371/journal.pone.0009367
pubmed: 20186336
pmcid: 2826413
Hao, L. Y., Giasson, B. I. & Bonini, N. M. DJ-1 is critical for mitochondrial function and rescues PINK1 loss of function. Proc. Natl Acad. Sci. USA 107, 9747–9752 (2010).
doi: 10.1073/pnas.0911175107
pubmed: 20457924
pmcid: 2906840
Burbulla, L. F. et al. Dopamine oxidation mediates mitochondrial and lysosomal dysfunction in Parkinson’s disease. Science 357, 1255–1261 (2017).
doi: 10.1126/science.aam9080
pubmed: 28882997
pmcid: 6021018
Ariga, H. et al. Neuroprotective function of DJ-1 in Parkinson’s disease. Oxid. Med. Cell. Longev. 2013, 683920 (2013).
doi: 10.1155/2013/683920
pubmed: 23766857
pmcid: 3671546
Pisetsky, D. S. The role of mitochondria in immune-mediated disease: the dangers of a split personality. Arthritis Res. Ther. 18, 169 (2016).
doi: 10.1186/s13075-016-1063-5
pubmed: 27424174
pmcid: 4947360
Mosley, R. L., Hutter-Saunders, J. A., Stone, D. K. & Gendelman, H. E. Inflammation and adaptive immunity in Parkinson’s disease. Cold Spring Harb. Perspect. Med. 2, a009381 (2012).
doi: 10.1101/cshperspect.a009381
pubmed: 22315722
pmcid: 3253034
Waak, J. et al. Regulation of astrocyte inflammatory responses by the Parkinson’s disease-associated gene DJ-1. FASEB J. 23, 2478–2489 (2009).
doi: 10.1096/fj.08-125153
pubmed: 19276172
Kim, J. H. et al. DJ-1 facilitates the interaction between STAT1 and its phosphatase, SHP-1, in brain microglia and astrocytes: a novel anti-inflammatory function of DJ-1. Neurobiol. Dis. 60, 1–10 (2013).
doi: 10.1016/j.nbd.2013.08.007
pubmed: 23969237
Amatullah, H. et al. DJ-1/PARK7 impairs bacterial clearance in sepsis. Am. J. Respir. Crit. Care Med. 195, 889–905 (2017).
doi: 10.1164/rccm.201604-0730OC
pubmed: 27735193
Liu, W. et al. Park7 interacts with p47
doi: 10.1038/cr.2015.63
pubmed: 26021615
pmcid: 4456629
Singh, Y. et al. Differential effect of DJ-1/PARK7 on development of natural and induced regulatory T cells. Sci. Rep. 5, 17723 (2015).
doi: 10.1038/srep17723
pubmed: 26634899
pmcid: 4669505
Sakaguchi, S., Miyara, M., Costantino, C. M. & Hafler, D. A. FOXP3
doi: 10.1038/nri2785
pubmed: 20559327
Reeve, A., Simcox, E. & Turnbull, D. Ageing and Parkinson’s disease: why is advancing age the biggest risk factor? Ageing Res. Rev. 14, 19–30 (2014).
doi: 10.1016/j.arr.2014.01.004
pubmed: 24503004
pmcid: 3989046
He, F. et al. PLAU inferred from a correlation network is critical for suppressor function of regulatory T cells. Mol. Syst. Biol. 8, 624 (2012).
doi: 10.1038/msb.2012.56
pubmed: 23169000
pmcid: 3531908
Bras, J., Guerreiro, R. & Hardy, J. SnapShot: genetics of Parkinson’s disease. Cell 160, 570 (2015).
doi: 10.1016/j.cell.2015.01.019
pubmed: 25635463
Gillis, J. & Pavlidis, P. The role of indirect connections in gene networks in predicting function. Bioinformatics 27, 1860–1866 (2011).
doi: 10.1093/bioinformatics/btr288
pubmed: 21551147
pmcid: 3117376
Pham, T. T. et al. DJ-1-deficient mice show less TH-positive neurons in the ventral tegmental area and exhibit non-motoric behavioural impairments. Genes Brain Behav. 9, 305–317 (2010).
doi: 10.1111/j.1601-183X.2009.00559.x
pubmed: 20039949
Jagger, A., Shimojima, Y., Goronzy, J. J. & Weyand, C. M. Regulatory T cells and the immune aging process: a mini-review. Gerontology 60, 130–137 (2014).
doi: 10.1159/000355303
pubmed: 24296590
Zeng, N. et al. DJ-1 depletion prevents immunoaging in T-cell compartments. EMBO Rep. 23, e53302 (2022).
doi: 10.15252/embr.202153302
pubmed: 35037711
pmcid: 8892345
Kohm, A. P., Carpentier, P. A., Anger, H. A. & Miller, S. D. Cutting edge: CD4
doi: 10.4049/jimmunol.169.9.4712
pubmed: 12391178
Mak, T. W. et al. Glutathione primes T cell metabolism for inflammation. Immunity 46, 675–689 (2017).
doi: 10.1016/j.immuni.2017.03.019
pubmed: 28423341
Gray, D. H. et al. Developmental kinetics, turnover, and stimulatory capacity of thymic epithelial cells. Blood 108, 3777–3785 (2006).
doi: 10.1182/blood-2006-02-004531
pubmed: 16896157
Zemmour, D. et al. Single-cell gene expression reveals a landscape of regulatory T cell phenotypes shaped by the TCR. Nat. Immunol. 19, 291–301 (2018).
doi: 10.1038/s41590-018-0051-0
pubmed: 29434354
pmcid: 6069633
Xu, J. et al. The Parkinson’s disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis. Hum. Mol. Genet. 14, 1231–1241 (2005).
doi: 10.1093/hmg/ddi134
pubmed: 15790595
Holling, T. M., Schooten, E. & van Den Elsen, P. J. Function and regulation of MHC class II molecules in T-lymphocytes: of mice and men. Hum. Immunol. 65, 282–290 (2004).
doi: 10.1016/j.humimm.2004.01.005
pubmed: 15120183
van der Brug, M. P. et al. RNA binding activity of the recessive parkinsonism protein DJ-1 supports involvement in multiple cellular pathways. Proc. Natl Acad. Sci. USA 105, 10244–10249 (2008).
doi: 10.1073/pnas.0708518105
pubmed: 18626009
pmcid: 2481328
Weyand, C. M., Goronzy, J. & Fathman, C. G. Modulation of CD4 by antigenic activation. J. Immunol. 138, 1351–1354 (1987).
pubmed: 3100638
Vandenbon, A. et al. Immuno-Navigator, a batch-corrected coexpression database, reveals cell type-specific gene networks in the immune system. Proc. Natl Acad. Sci. USA 113, E2393–E2402 (2016).
doi: 10.1073/pnas.1604351113
pubmed: 27078110
pmcid: 4855614
Patel, M. S. & Roche, T. E. Molecular biology and biochemistry of pyruvate dehydrogenase complexes. FASEB J. 4, 3224–3233 (1990).
doi: 10.1096/fasebj.4.14.2227213
pubmed: 2227213
Desdin-Mico, G. et al. T cells with dysfunctional mitochondria induce multimorbidity and premature senescence. Science 368, 1371–1376 (2020).
doi: 10.1126/science.aax0860
pubmed: 32439659
Wang, R. & Green, D. R. Metabolic checkpoints in activated T cells. Nat. Immunol. 13, 907–915 (2012).
doi: 10.1038/ni.2386
Zhou, Z. H., McCarthy, D. B., O’Connor, C. M., Reed, L. J. & Stoops, J. K. The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes. Proc. Natl Acad. Sci. USA 98, 14802–14807 (2001).
doi: 10.1073/pnas.011597698
pubmed: 11752427
pmcid: 64939
Zachar, Z. et al. Non-redox-active lipoate derivates disrupt cancer cell mitochondrial metabolism and are potent anticancer agents in vivo. J. Mol. Med. 89, 1137–1148 (2011).
doi: 10.1007/s00109-011-0785-8
pubmed: 21769686
Polansky, J. K. et al. DNA methylation controls Foxp3 gene expression. Eur. J. Immunol. 38, 1654–1663 (2008).
doi: 10.1002/eji.200838105
pubmed: 18493985
Benayoun, B. A., Pollina, E. A. & Brunet, A. Epigenetic regulation of ageing: linking environmental inputs to genomic stability. Nat. Rev. Mol. Cell Biol. 16, 593–610 (2015).
doi: 10.1038/nrm4048
pubmed: 26373265
pmcid: 4736728
Gerriets, V. A. et al. Metabolic programming and PDHK1 control CD4
doi: 10.1172/JCI76012
pubmed: 25437876
Richard, A. J., Hang, H. & Stephens, J. M. Pyruvate dehydrogenase complex (PDC) subunits moonlight as interaction partners of phosphorylated STAT5 in adipocytes and adipose tissue. J. Biol. Chem. 292, 19733–19742 (2017).
doi: 10.1074/jbc.M117.811794
pubmed: 28982698
pmcid: 5712614
Patel, K. P., O’Brien, T. W., Subramony, S. H., Shuster, J. & Stacpoole, P. W. The spectrum of pyruvate dehydrogenase complex deficiency: clinical, biochemical and genetic features in 371 patients. Mol. Genet. Metab. 106, 385–394 (2012).
doi: 10.1016/j.ymgme.2012.03.017
pubmed: 22896851
pmcid: 4003492
Olahova, M. et al. Biallelic mutations in ATP5F1D, which encodes a subunit of ATP synthase, cause a metabolic disorder. Am. J. Hum. Genet. 102, 494–504 (2018).
doi: 10.1016/j.ajhg.2018.01.020
pubmed: 29478781
pmcid: 6117612
Probst-Kepper, M. et al. GARP: a key receptor controlling FOXP3 in human regulatory T cells. J. Cell. Mol. Med. 13, 3343–3357 (2009).
doi: 10.1111/j.1582-4934.2009.00782.x
pubmed: 19453521
pmcid: 4516490
Tyanova, S. et al. The Perseus computational platform for comprehensive analysis of (prote)omics data. Nat. Methods 13, 731–740 (2016).
doi: 10.1038/nmeth.3901
pubmed: 27348712