mitoNEET as a novel drug target for mitochondrial dysfunction

Drug Discovery Today

Volumn 19, Issue 10, 2014, Pages 1601-1606

  Geldenhuys, Werner J ^a   Leeper, Thomas C ^b   Carroll, Richard T ^a  

^a NORTHEAST OHIO MEDICAL UNIVERSITY   (United States)

^b UNIVERSITY OF AKRON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; MITOCHONDRIAL PROTEIN; MITOCHONDRIAL PROTEIN MITONEET; MITONEET LIGAND; UNCLASSIFIED DRUG; 2,4 THIAZOLIDINEDIONE DERIVATIVE; CISD1 PROTEIN, HUMAN;

BIOENERGY; BIOLOGICAL ACTIVITY; BREAST CANCER; CELL ENERGY; DIABETES MELLITUS; DISORDERS OF MITOCHONDRIAL FUNCTIONS; DRUG DESIGN; DRUG TARGETING; HUMAN; INFLAMMATION; MITOCHONDRION; NERVE DEGENERATION; NONHUMAN; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; REVIEW; ANIMAL; CHEMISTRY; DRUG DELIVERY SYSTEM; ENERGY METABOLISM; METABOLISM; PROTEIN CONFORMATION;

ANIMALS; DRUG DELIVERY SYSTEMS; ENERGY METABOLISM; HUMANS; MITOCHONDRIA; MITOCHONDRIAL PROTEINS; PROTEIN CONFORMATION; THIAZOLIDINEDIONES;

EID: 84908615741     PISSN: 13596446     EISSN: 18785832     Source Type: Journal    
DOI: 10.1016/j.drudis.2014.05.001     Document Type: Review

References (64)

1. Perez-Pinzon, M.A. et al. (2012) Novel mitochondrial targets for neuroprotection. J. Cereb. Blood Flow Metab. 32, 1362-1376
2. Soane, L. et al. (2007) Mechanisms of impaired mitochondrial energy metabolism in acute and chronic neurodegenerative disorders. J. Neurosci. Res. 85, 3407-3415
3. Yonutas, H.M. and Sullivan, P.G. (2013) Targeting PPAR isoforms following CNS injury. Curr. Drug Targets 14, 733-742
4. Sullivan, P.G. et al. (2004) Mitochondrial uncoupling as a therapeutic target following neuronal injury. J. Bioenerg. Biomembr. 36, 353-356
5. Sullivan, P.G. et al. (2005) Mitochondrial permeability transition in CNS trauma: cause or effect of neuronal cell death? J. Neurosci. Res. 79, 231-239
6. Youdim, M.B. and Oh, Y.J. (2013) Promise of neurorestoration and mitochondrial biogenesis in Parkinson's disease with multi target drugs: an alternative to stem cell therapy. Exp. Neurobiol. 22, 167-172
7. Beal, M.F. (2005) Mitochondria take center stage in aging and neurodegeneration. Ann. Neurol. 58, 495-505
8. Reeve, A. et al. (2014) Ageing and Parkinson's disease: why is advancing age the biggest risk factor? Ageing Res. Rev. 14C, 19-30
9. Abou-Sleiman, P.M. et al. (2006) Expanding insights of mitochondrial dysfunction in Parkinson's disease. Nat. Rev. Neurosci. 7, 207-219
10. Johri, A. and Beal, M.F. (2012) Mitochondrial dysfunction in neurodegenerative diseases. J. Pharmacol. Exp. Ther. 342, 619-630
11. Murphy, M.P. (2009) How mitochondria produce reactive oxygen species. Biochem. J. 417, 1-13
12. Kushnareva, Y. et al. (2002) Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation-reduction state. Biochem. J. 368, 545-553
13. Szendroedi, J. et al. (2012) The role of mitochondria in insulin resistance and type 2 diabetes mellitus. Nat. Rev. Endocrinol. 8, 92-103
14. Wenner, C.E. (2012) Targeting mitochondria as a therapeutic target in cancer. J. Cell Physiol. 227, 450-456
15. Kusminski, C.M. et al. (2012) MitoNEET-driven alterations in adipocyte mitochondrial activity reveal a crucial adaptive process that preserves insulin sensitivity in obesity. Nat. Med. 18, 1539-1549
16. Salem, A.F. et al. (2012) Mitochondrial biogenesis in epithelial cancer cells promotes breast cancer tumor growth and confers autophagy resistance. Cell Cycle 11, 4174-4180
17. Wiley, S.E. et al. (2007) MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity. Proc. Natl. Acad. Sci. U. S. A. 104, 5318-5323
18. Colca, J.R. et al. (2004) Identification of a novel mitochondrial protein (mitoNEET) cross-linked specifically by a thiazolidinedione photoprobe. Am. J. Physiol. Endocrinol. Metab. 286, E252-E260
19. Harrigan, G.G. et al. (2006) PNU-91325 increases fatty acid synthesis from glucose and mitochondrial long chain fatty acid degradation: a comparative tracer-based metabolomics study with rosiglitazone and pioglitazone in HepG2 cells. Metabolomics 2, 21-29
20. Feinstein, D.L. et al. (2005) Receptor-independent actions of PPAR thiazolidinedione agonists: is mitochondrial function the key? Biochem. Pharmacol. 70, 177-188
21. Lin, J. et al. (2007) Crystal structure of human mitoNEET reveals distinct groups of iron sulfur proteins. Proc. Natl. Acad. Sci. U. S. A. 104, 14640-14645
22. Paddock, M.L. et al. (2007) MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone. Proc. Natl. Acad. Sci. U. S. A. 104, 14342-14347
23. Hou, X. et al. (2007) Crystallographic studies of human MitoNEET. J. Biol. Chem. 282, 33242-33246
24. Kounosu, A. et al. (2008) Crystallization and preliminary X-ray diffraction studies of the prototypal homologue of mitoNEET (Tth-NEET0026) from the extreme thermophile Thermus thermophilus HB8. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64, 1146-1148
25. Nechushtai, R. et al. (2012) Characterization of Arabidopsis NEET reveals an ancient role for NEET proteins in iron metabolism. Plant Cell 24, 2139-2154
26. Wiley, S.E. et al. (2007) The outer mitochondrial membrane protein mitoNEET contains a novel redox-active 2Fe-2S cluster. J. Biol. Chem. 282, 23745-23749
27. Zuris, J.A. et al. (2011) Facile transfer of [2Fe-2S] clusters from the diabetes drug target mitoNEET to an apo-acceptor protein. Proc. Natl. Acad. Sci. U. S. A. 108, 13047-13052
28. Conlan, A.R. et al. (2011) Mutation of the His ligand in mitoNEET stabilizes the 2Fe-2S cluster despite conformational heterogeneity in the ligand environment. Acta Crystallogr. D Biol. Crystallogr. 67, 516-523
29. Lin, J. et al. (2011) Structure and molecular evolution of CDGSH iron-sulfur domains. PLoS One 6, e24790
30. Conlan, A.R. et al. (2009) Crystal structure of Miner1: the redox-active 2Fe-2S protein causative in Wolfram syndrome 2. J. Mol. Biol. 392, 143-153
31. Chang, N.C. et al. (2012) Bcl-2-associated autophagy regulator Naf-1 required for maintenance of skeletal muscle. Hum. Mol. Genet. 21, 2277-2287
32. 2+ homeostasis. EMBO Mol. Med. 5, 904-918
33. Chang, N.C. et al. (2012) BCL2-CISD2: an ER complex at the nexus of autophagy and calcium homeostasis? Autophagy 8, 856-857
34. Wu, C.Y. et al. (2012) A persistent level of Cisd2 extends healthy lifespan and delays aging in mice. Hum. Mol. Genet. 21, 3956-3968
35. Chen, Y.F. et al. (2009) Cisd2 mediates mitochondrial integrity and life span in mammals. Autophagy 5, 1043-1045
36. Chen, Y.F. et al. (2009) Cisd2 deficiency drives premature aging and causes mitochondria-mediated defects in mice. Genes Dev. 23, 1183-1194
37. Akar, C. et al. (2010) Receptor-independent metabolic effects of thiazolidinediones in astrocytes. Open Cancer Immunol. J. 3, 36-40
38. Lazarou, M. et al. (2013) PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding. J. Cell Biol. 200, 163-172
39. Brand, M.D. and Nicholls, D.G. (2011) Assessing mitochondrial dysfunction in cells. Biochem. J. 435, 297-312
40. Simoneau, J.A. et al. (1999) Markers of capacity to utilize fatty acids in human skeletal muscle: relation to insulin resistance and obesity and effects of weight loss. FASEB J. 13, 2051-2060
41. Sohn, Y.S. et al. (2013) NAF-1 and mitoNEET are central to human breast cancer proliferation by maintaining mitochondrial homeostasis and promoting tumor growth. Proc. Natl. Acad. Sci. U. S. A. 110, 14676-14681
42. Chung, H.H. et al. (2013) The relationship between metformin and cancer in patients with type 2 diabetes. Diabetes Metab. J. 37, 125-131
43. Sanz, M.N. et al. (2011) Acute mitochondrial actions of glitazones on the liver: a crucial parameter for their antidiabetic properties. Cell Physiol. Biochem. 28, 899-910
44. Colca, J.R. et al. (2013) Clinical proof-of-concept study with MSDC-0160, a prototype mTOT-modulating insulin sensitizer. Clin. Pharmacol. Ther. 93, 352-359
45. Bolten, C.W. et al. (2007) Insulin sensitizing pharmacology of thiazolidinediones correlates with mitochondrial gene expression rather than activation of PPAR gamma. Gene Regul. Syst. Biol. 1, 73-82
46. Chen, Z. et al. (2012) Insulin resistance and metabolic derangements in obese mice are ameliorated by a novel peroxisome proliferator-activated receptor gamma-sparing thiazolidinedione. J. Biol. Chem. 287, 23537-23548
47. Guan, Y. et al. (2005) Thiazolidinediones expand body fluid volume through PPARgamma stimulation of ENaC-mediated renal salt absorption. Nat. Med. 11, 861-866
48. Colca, J.R. et al. (2013) Identification of a mitochondrial target of thiazolidinedione insulin sensitizers (mTOT)-relationship to newly identified mitochondrial pyruvate carrier proteins. PLoS One 8, e61551
49. Divakaruni, A.S. et al. (2013) Thiazolidinediones are acute, specific inhibitors of the mitochondrial pyruvate carrier. Proc. Natl. Acad. Sci. U. S. A. 110, 5422-5427
50. Garcia-Ruiz, I. et al. (2013) Pioglitazone leads to an inactivation and disassembly of complex I of the mitochondrial respiratory chain. BMC Biol. 11, 88
51. Roberts, M.E. et al. (2013) Identification of disulfide bond formation between mitoNEET and glutamate dehydrogenase 1. Biochemistry 52, 8969-8971
52. Li, M. et al. (2012) The structure and allosteric regulation of mammalian glutamate dehydrogenase. Arch. Biochem. Biophys. 519, 69-80
53. Hunter, R.L. et al. (2008) Protective properties afforded by pioglitazone against intrastriatal LPS in Sprague-Dawley rats. Neurosci. Lett. 432, 198-201
54. Shulga, N. and Pastorino, J.G. (2014) Mitoneet mediates TNFα-induced necroptosis promoted by fructose and ethanol exposure. J. Cell Sci. 127, 896-907
55. Takeda, K. et al. (2001) 15-Deoxy-delta 12,14-prostaglandin J2 and thiazolidinediones activate the MEK/ERK pathway through phosphatidylinositol 3-kinase in vascular smooth muscle cells. J. Biol. Chem. 276, 48950-48955
56. Bolden, A. et al. (2012) The PPAR gamma agonist troglitazone regulates Erk 1/2 phosphorylation via a PPARgamma-independent, MEK-dependent pathway in human prostate cancer cells. PPAR Res. 2012, 929052
57. Chen, Y. and Dorn, G.W., 2nd (2013) PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria. Science 340, 471-475
58. Tanaka, A. (2010) Parkin-mediated selective mitochondrial autophagy, mitophagy: Parkin purges damaged organelles from the vital mitochondrial network. FEBS Lett. 584, 1386-1392
59. Tamir, S. et al. (2013) Nutrient-deprivation autophagy factor-1 (NAF-1): biochemical properties of a novel cellular target for anti-diabetic drugs. PLoS One 8, e61202
60. Geldenhuys, W.J. et al. (2011) A novel binding assay identifies high affinity ligands to the rosiglitazone binding site of mitoNEET. Bioorg. Med. Chem. Lett. 21, 5498-5501
61. Arif, W. et al. (2011) Complexes of the outer mitochondrial membrane protein mitoNEET with resveratrol-3-sulfate. Biochemistry 50, 5806-5811
62. Geldenhuys, W.J. et al. (2010) Structure-based design of a thiazolidinedione which targets the mitochondrial protein mitoNEET. Bioorg. Med. Chem. Lett. 20, 819-823
63. Brunmair, B. et al. (2004) Thiazolidinediones, like metformin, inhibit respiratory complex I: a common mechanism contributing to their antidiabetic actions? Diabetes 53, 1052-1059
64. Fujisawa, K. et al. (2009) TZDs reduce mitochondrial ROS production and enhance mitochondrial biogenesis. Biochem. Biophys. Res. Commun. 379, 43-48