Erratum: Deficiency of Parkinson's disease-related gene Fbxo7 is associated with impaired mitochondrial metabolism by PARP activation (Cell Death and Differentiation (2017) 24 (120-131) DOI: 10.1038/cdd.2016.104);Deficiency of Parkinson's disease-related gene Fbxo7 is associated with impaired mitochondrial metabolism by PARP activation

Cell Death and Differentiation

Volumn 24, Issue 1, 2017, Pages 120-131

  Delgado Camprubi, Marta ^a   Esteras, Noemi ^a   Soutar, Marc Pm ^a   Plun Favreau, Helene ^a   Abramov, Andrey Y ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; F BOX ONLY PROTEIN 7; F BOX PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE INHIBITOR; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UNCLASSIFIED DRUG; 3,4-DIHYDRO-5-(4-(1-PIPERIDINYL)BUTOXY)-1(2H)-ISOQUINOLINONE; FBXO7 PROTEIN, HUMAN; IODOACETIC ACID; ISOQUINOLINE DERIVATIVE; PIPERIDINE DERIVATIVE; SMALL INTERFERING RNA; SODIUM CYANIDE;

ARTICLE; CELL LEVEL; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; FIBROBLAST; GENE MUTATION; GENE SILENCING; HUMAN; HUMAN CELL; HUMAN TISSUE; MITOCHONDRIAL MEMBRANE POTENTIAL; MITOCHONDRIAL RESPIRATION; MOLECULAR PATHOLOGY; NEUROBLASTOMA CELL LINE; NORMAL HUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN DEFECT; RESPIRATORY CHAIN; ANTAGONISTS AND INHIBITORS; CELL CULTURE; CHEMISTRY; DRUG EFFECTS; GENETICS; METABOLISM; MITOCHONDRION; MITOPHAGY; OXYGEN CONSUMPTION; PATHOLOGY; RNA INTERFERENCE; SINGLE NUCLEOTIDE POLYMORPHISM;

ADENOSINE TRIPHOSPHATE; CELLS, CULTURED; ELECTRON TRANSPORT COMPLEX I; F-BOX PROTEINS; HUMANS; IODOACETIC ACID; ISOQUINOLINES; MEMBRANE POTENTIAL, MITOCHONDRIAL; MITOCHONDRIA; MITOCHONDRIAL DEGRADATION; NAD; OXYGEN CONSUMPTION; PARKINSON DISEASE; PIPERIDINES; POLY(ADP-RIBOSE) POLYMERASE INHIBITORS; POLY(ADP-RIBOSE) POLYMERASES; POLYMORPHISM, SINGLE NUCLEOTIDE; REACTIVE OXYGEN SPECIES; RNA INTERFERENCE; RNA, SMALL INTERFERING; SODIUM CYANIDE;

EID: 84989266728     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2017.175     Document Type: Erratum

References (59)

1. Burchell VS, Gandhi S, Deas E, Wood NW, Abramov AY, Plun-Favreau H. Targeting mitochondrial dysfunction in neurodegenerative disease: part II. Expert Opin Ther Targets 2010; 14: 497-511.
2. Bekris LM, Mata IF, Zabetian CP. The genetics of Parkinson disease. J Geriatr Psychiatry Neurol 2010; 23: 228-242.
3. Martinez TN, Greenamyre JT. Toxin models of mitochondrial dysfunction in Parkinson's disease. Antioxid Redox Signal 2012; 16: 920-934.
4. Hisahara S, Shimohama S. Toxin-induced, genetic animal models of Parkinson's disease. Parkinsons Dis 2010; 2011: 951709.
5. Hargreaves IP, Lane A, Sleiman PMA. The coenzyme Q10 status of the brain regions of Parkinson's disease patients. Neurosci Lett 2008; 447: 17-19.
6. Parker WD, Parks JK, Swerdlow RH. Complex I deficiency in Parkinson's disease frontal cortex. Brain Res 2008; 1189: 215-218.
7. Schapira AH V. Mitochondria in the aetiology, pathogenesis of Parkinson's disease. Lancet Neurol 2008; 7: 97-109.
8. Abramov AY, Gegg M, Grunewald A, Wood NW, Klein C, Schapira AHV. Bioenergetic consequences of PINK1 mutations in Parkinson disease. PLoS One 2011; 6: e25622.
9. Björkblom B, Maple-Grødem J, Puno MR, Odell M, Larsen JP, Møller SG. Reactive oxygen species-mediated DJ-1 monomerization modulates intracellular trafficking involving karyopherin ?2. Mol Cell Biol 2014; 34: 3024-3040.
10. Fitzgerald JC, Camprubi MD, Dunn L, Wu H-C, Ip NY, Kruger R et al. Phosphorylation of HtrA2 by cyclin-dependent kinase-5 is important for mitochondrial function. Cell Death Differ 2012; 19: 257-266.
11. Pickrell AM, Youle RJ. The roles of PINK1, parkin, mitochondrial fidelity in Parkinson's disease. Neuron 2015; 85: 257-273.
12. Di Fonzo A, Dekker MCJ, Montagna P, Baruzzi A, Yonova EH, Correia Guedes L et al. FBXO7 mutations cause autosomal recessive, early-onset parkinsonian-pyramidal syndrome. Neurology 2009; 72: 240-245.
13. Skowyra D, Craig KL, Tyers M, Elledge SJ, Harper JW. F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 1997; 91: 209-219.
14. Bai C, Sen P, Hofmann K, Ma L, Goebl M, Harper JW et al. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 1996; 86: 263-274.
15. Nelson DE, Randle SJ, Laman H. Beyond ubiquitination: the atypical functions of Fbxo7, other F-box proteins. Open Biol 2013; 3: 130131.
16. Burchell VS, Nelson DE, Sanchez-Martinez A, Delgado-Camprubi M, Ivatt RM, Pogson JH et al. The Parkinson's disease-linked proteins Fbxo7, Parkin interact to mediate mitophagy. Nat Neurosci 2013; 16: 1257-1265.
17. Moroni F. Poly(ADP-ribose)polymerase 1 (PARP-1), postischemic brain damage. Curr Opin Pharmacol 2008; 8: 96-103.
18. Diefenbach J, Bürkle A. Introduction to poly(ADP-ribose) metabolism. Cell Mol Life Sci 2005; 62: 721-730.
19. Abeti R, Abramov AY, Duchen MR. Beta-amyloid activates PARP causing astrocytic metabolic failure, neuronal death. Brain 2011; 134(Pt 6): 1658-1672.
20. Cecchi C, Fiorillo C, Sorbi S, Latorraca S, Nacmias B, Bagnoli S et al. Oxidative stress, reduced antioxidant defenses in peripheral cells from familial Alzheimer's patients. Free Radic Biol Med 2002; 33: 1372-1379.
21. Love S, Barber R, Wilcock GK. Increased poly(ADP-ribosyl)ation of nuclear proteins in Alzheimer's disease. Brain 1999; 122(Pt 2): 247-253.
22. Abramov AY, Duchen MR. Mechanisms underlying the loss of mitochondrial membrane potential in glutamate excitotoxicity. Biochim Biophys Acta 2008; 1777: 953-964.
23. Duan Y, Gross RA, Sheu S-S. Ca2+-dependent generation of mitochondrial reactive oxygen species serves as a signal for poly(ADP-ribose) polymerase-1 activation during glutamate excitotoxicity. J Physiol 2007; 585(Pt 3): 741-758.
24. Brand MD, Nicholls DG. Assessing mitochondrial dysfunction in cells. Biochem J 2011; 435: 297-312.
25. Adachi K, Oiwa K, Nishizaka T, Furuike S, Noji H, Itoh H et al. Coupling of rotation, catalysis in F(1)-ATPase revealed by single-molecule imaging, manipulation. Cell 2007; 130: 309-321.
26. Jonckheere AI, Smeitink JAM, Rodenburg RJT. Mitochondrial ATP synthase: architecture, function, pathology. J Inherit Metab Dis 2012; 35: 211-225.
27. Berndt N, Holzhütter H-G, Bulik S. Implications of enzyme deficiencies on mitochondrial energy metabolism, reactive oxygen species formation of neurons involved in rotenoneinduced Parkinson's disease: a model-based analysis. FEBS J 2013; 280: 5080-5093.
28. Murphy MP. How mitochondria produce reactive oxygen species. Biochem J 2009; 417: 1-13.
29. Tretter L, Sipos I, Adam-Vizi V. Initiation of neuronal damage by complex I deficiency, oxidative stress in Parkinson's disease. Neurochem Res 2004; 29: 569-577.
30. Bartolomé F, Abramov AY. Measurement of mitochondrial NADH, FAD autofluorescence in live cells. Methods Mol Biol 2015; 1264: 263-270.
31. Gandhi S, Wood-Kaczmar A, Yao Z, Plun-Favreau H, Deas E, Klupsch K et al. PINK1-associated Parkinson's disease is caused by neuronal vulnerability to calcium-induced cell death. Mol Cell 2009; 33: 627-638.
32. Houtkooper RH, Cantó C, Wanders RJ, Auwerx J. The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways. Endocr Rev 2010; 31: 194-223.
33. Alano CC, Garnier P, Ying W, Higashi Y, Kauppinen TM, Swanson RA. NAD+ depletion is necessary, sufficient for poly(ADP-ribose) polymerase-1-mediated neuronal death. J Neurosci 2010; 30: 2967-2978.
34. Bai P, Cantó C. The role of PARP-1, PARP-2 enzymes in metabolic regulation, disease. Cell Metab 2012; 16: 290-295.
35. Wang S, Yang X, Lin Y, Qiu X, Li H, Zhao X et al. Cellular NAD depletion, decline of SIRT1 activity play critical roles in PARP-1-mediated acute epileptic neuronal death in vitro. Brain Res 2013; 1535: 14-23.
36. Wang S, Xing Z, Vosler PS, Yin H, Li W, Zhang F et al. Cellular NAD replenishment confers marked neuroprotection against ischemic cell death: role of enhanced DNA repair. Stroke 2008; 39: 2587-2595.
37. Scalia M, Satriano C, Greca R, Stella AMG, Rizzarelli E, Spina-Purrello V. PARP-1 inhibitors DPQ, PJ-34 negatively modulate proinflammatory commitment of human glioblastoma cells. Neurochem Res 2013; 38: 50-58.
38. Song Z-F, Ji X-P, Li X-X, Wang S-J, Wang S-H, Zhang Y. Inhibition of the activity of poly (ADP-ribose) polymerase reduces heart ischaemia/reperfusion injury via suppressing JNKmediated AIF translocation. J Cell Mol Med 2008; 12: 1220-1228.
39. Wang G, Huang X, Li Y, Guo K, Ning P, Zhang Y. PARP-1 inhibitor, DPQ, attenuates LPS-induced acute lung injury through inhibiting NF-?B-mediated inflammatory response. PLoS One 2013; 8: e79757.
40. Abramov AY, Duchen MR. Impaired mitochondrial bioenergetics determines glutamateinduced delayed calcium deregulation in neurons. Biochim Biophys Acta 2010; 1800: 297-304.
41. Plun-Favreau H, Burchell VS, Holmström KM, Yao Z, Deas E, Cain K et al. HtrA2 deficiency causes mitochondrial uncoupling through the F1F1-ATP synthase, consequent ATP depletion. Cell Death Dis 2012; 3: e335.
42. Schapira AH, Cooper JM, Dexter D, Jenner P, Clark JB, Marsden CD. Mitochondrial complex I deficiency in Parkinson's disease. Lancet 1989; 1: 1269.
43. Lee Y, Karuppagounder SS, Shin J-H, Lee Y-I, Ko HS, Swing D et al. Parthanatos mediates AIMP2-activated age-dependent dopaminergic neuronal loss. Nat Neurosci 2013; 16: 1392-1400.
44. Martire S, Mosca L, d'Erme M. PARP-1 involvement in neurodegeneration: A focus on Alzheimer's, Parkinson's diseases. Mech Ageing Dev 2015; 146-148C: 53-64.
45. Outeiro TF, Grammatopoulos TN, Altmann S, Amore A, Standaert DG, Hyman BT et al. Pharmacological inhibition of PARP-1 reduces alpha-synuclein-, MPP+-induced cytotoxicity in Parkinson's disease in vitro models. Biochem Biophys Res Commun 2007; 357: 596-602.
46. Chen M, Zsengellér Z, Xiao C-Y, Szabó C. Mitochondrial-to-nuclear translocation of apoptosis-inducing factor in cardiac myocytes during oxidant stress: potential role of poly (ADP-ribose) polymerase-1. Cardiovasc Res 2004; 63: 682-688.
47. Yu S-W, Wang H, Poitras MF, Coombs C, Bowers WJ, Federoff HJ et al. Mediation of poly (ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor. Science 2002; 297: 259-263.
48. Ying W, Garnier P, Swanson RA. NAD+ repletion prevents PARP-1-induced glycolytic blockade, cell death in cultured mouse astrocytes. Biochem Biophys Res Commun 2003; 308: 809-813.
49. Andrabi SA, Umanah GKE, Chang C, Stevens DA, Karuppagounder SS, Gagné J-P et al. Poly(ADP-ribose) polymerase-dependent energy depletion occurs through inhibition of glycolysis. Proc Natl Acad Sci USA 2014; 111: 10209-10214.
50. Fouquerel E, Goellner EM, Yu Z, Gagné J-P, Barbi de Moura M, Feinstein T et al. ARTD1/PARP1 negatively regulates glycolysis by inhibiting hexokinase 1 independent of NAD(+) depletion. Cell Rep 2014; 8: 1819-1831.
51. Baek S-H, Bae O-N, Kim E-K, Yu S-W. Induction of mitochondrial dysfunction by poly(ADPribose) polymer: implication for neuronal cell death. Mol Cell 2013; 36: 258-266.
52. Niere M, Kernstock S, Koch-Nolte F, Ziegler M. Functional localization of two poly(ADP-ribose)-degrading enzymes to the mitochondrial matrix. Mol Cell Biol 2008; 28: 814-824.
53. Lagouge M, Argmann C, Gerhart-Hines Z, Meziane H, Lerin C, Daussin F et al. Resveratrol improves mitochondrial function, protects against metabolic disease by activating SIRT1, PGC-1alpha. Cell 2006; 127: 1109-1122.
54. Lee IH, Cao L, Mostoslavsky R, Lombard DB, Liu J, Bruns NE et al. A role for the NADdependent deacetylase Sirt1 in the regulation of autophagy. Proc Natl Acad Sci USA 2008; 105: 3374-3379.
55. Brunet A, Sweeney LB, Sturgill JF, Chua KF, Greer PL, Lin Y et al. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 2004; 303: 2011-2015.
56. Ahn B-H, Kim H-S, Song S, Lee IH, Liu J, Vassilopoulos A et al. A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Proc Natl Acad Sci USA 2008; 105: 14447-14452.
57. Finley LWS, Haas W, Desquiret-Dumas V, Wallace DC, Procaccio V, Gygi SP et al. Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase activity. PLoS One 2011; 6: e23295.
58. Shulga N, Pastorino JG. Hexokinase II binding to Mitochondria is Necessary for Kupffer cell Activation, is Potentiated by Ethanol Exposure. J Biol Chem 2014; 289: 26213-2.
59. Cantó C, Auwerx J. Targeting sirtuin 1 to improve metabolism: all you need is NAD(+)? Pharmacol Rev 2012; 64: 166-187.