The Human Cytochrome c Oxidase Assembly Factors SCO1 and SCO2 Have Regulatory Roles in the Maintenance of Cellular Copper Homeostasis (DOI:10.1016/j.cmet.2006.12.001);The Human Cytochrome c Oxidase Assembly Factors SCO1 and SCO2 Have Regulatory Roles in the Maintenance of Cellular Copper Homeostasis

Cell Metabolism

Volumn 5, Issue 1, 2007, Pages 9-20

  Leary, Scot C ^a,b   Cobine, Paul A ^c   Kaufman, Brett A ^a,b   Guercin, Guy Hellen ^a,b   Mattman, Andre ^d   Palaty, Jan ^d   Lockitch, Gillian ^d   Winge, Dennis R ^c   Rustin, Pierre ^e   Horvath, Rita ^f   Shoubridge, Eric A ^a,b  

^a MCGILL UNIVERSITY   (Canada)

^b MCGILL UNIVERSITY   (Canada)

^c UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^d CHILDREN S AND WOMEN S HEALTH CENTRE OF BRITISH COLUMBIA   (Canada)

^e INSERM   (France)

^f Institute of Clinical Chemistry Molecular Diagnostics and Mitochondrial Genetics   (Germany)

Author keywords

HUMDISEASE

Indexed keywords

COPPER; CYTOCHROME C OXIDASE; MUTANT PROTEIN; PROTEIN SCO1; PROTEIN SCO2; SHORT HAIRPIN RNA;

ALLELE; ARTICLE; CONTROLLED STUDY; COPPER DEFICIENCY; FIBROBLAST; GENE MUTATION; GENE OVEREXPRESSION; HOMEOSTASIS; HUMAN; HUMAN CELL; HUMAN TISSUE; METAL BINDING; MITOCHONDRION; OXIDATION REDUCTION STATE; PHENOTYPE; PRIORITY JOURNAL; PROTEIN FUNCTION; SIGNAL TRANSDUCTION; WILD TYPE;

EID: 33845596232     PISSN: 15504131     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cmet.2007.04.002     Document Type: Erratum

References (37)

1. Antonicka H., Leary S.C., Guercin G.H., Agar J.N., Horvath R., Kennaway N.G., Harding C.O., Jaksch M., and Shoubridge E.A. Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency. Hum. Mol. Genet. 12 (2003) 2693-2702
2. Banci L., Bertini I., Calderone V., Ciofi-Baffoni S., Mangani S., Martinelli M., Palumaa P., and Wang S. A hint for the function of human Sco1 from different structures. Proc. Natl. Acad. Sci. USA 103 (2006) 8595-8600
3. Chinenov Y.V. Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes. J. Mol. Med. 78 (2000) 239-242
4. Cobine P.A., Ojeda L.D., Rigby K.M., and Winge D.R. Yeast contain a non-proteinaceous pool of copper in the mitochondrial matrix. J. Biol. Chem. 279 (2004) 14447-14455
5. Cobine P.A., Pierrel F., Bestwick M.L., and Winge D.R. Mitochondrial matrix copper complex used in metallation of cytochrome oxidase and superoxide dismutase. J. Biol. Chem. 281 (2006) 36552-36559
6. Cobine P.A., Pierrel F., Leary S.C., Sasarman F., Horng Y.C., Shoubridge E.A., and Winge D.R. The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding. J. Biol. Chem. 281 (2006) 12270-12276
7. Cobine P.A., Pierrel F., and Winge D.R. Copper trafficking to the mitochondrion and assembly of copper metalloenzymes. Biochim. Biophys. Acta 1763 (2006) 759-772
8. Fox P.L. The copper-iron chronicles: the story of an intimate relationship. Biometals 16 (2003) 9-40
9. Freisinger P., Horvath R., Macmillan C., Peters J., and Jaksch M. Reversion of hypertrophic cardiomyopathy in a patient with deficiency of the mitochondrial copper binding protein Sco2: is there a potential effect of copper?. J. Inherit. Metab. Dis. 27 (2004) 67-79
10. Guo Y., Smith K., and Petris M.J. Cisplatin stabilizes a multimeric complex of the human Ctr1 copper transporter: requirement for the extracellular methionine-rich clusters. J. Biol. Chem. 279 (2004) 46393-46399
11. Hamza I., and Gitlin J.D. Copper chaperones for cytochrome c oxidase and human disease. J. Bioenerg. Biomembr. 34 (2002) 381-388
12. Horng Y.C., Leary S.C., Cobine P.A., Young F.B., George G.N., Shoubridge E.A., and Winge D.R. Human Sco1 and Sco2 function as copper-binding proteins. J. Biol. Chem. 280 (2005) 34113-34122
13. Hung I.H., Suzuki M., Yamaguchi Y., Yuan D.S., Klausner R.D., and Gitlin J.D. Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 272 (1997) 21461-21466
14. Ishida S., Lee J., Thiele D.J., and Herskowitz I. Uptake of the anticancer drug cisplatin mediated by the copper transporter Ctr1 in yeast and mammals. Proc. Natl. Acad. Sci. USA 99 (2002) 14298-14302
15. Jaksch M., Ogilvie I., Yao J., Kortenhaus G., Bresser H.G., Gerbitz K.D., and Shoubridge E.A. Mutations in SCO2 are associated with a distinct form of hypertrophic cardiomyopathy and cytochrome c oxidase deficiency. Hum. Mol. Genet. 9 (2000) 795-801
16. Jaksch M., Horvath R., Horn N., Auer D.P., Macmillan C., Peters J., Gerbitz K.D., Kraegeloh-Mann I., Muntau A., Karcagi V., et al. Homozygosity (E140K) in SCO2 causes delayed infantile onset of cardiomyopathy and neuropathy. Neurology 57 (2001) 1440-1446
17. Jaksch M., Paret C., Stucka R., Horn N., Muller-Hocker J., Horvath R., Trepesch N., Stecker G., Freisinger P., Thirion C., et al. Cytochrome c oxidase deficiency due to mutations in SCO2, encoding a mitochondrial copper-binding protein, is rescued by copper in human myoblasts. Hum. Mol. Genet. 10 (2001) 3025-3035
18. Klomp A.E., Juijn J.A., van der Gun L.T., van den Berg I.E., Berger R., and Klomp L.W. The N-terminus of the human copper transporter 1 (hCTR1) is localized extracellularly, and interacts with itself. Biochem. J. 370 (2003) 881-889
19. Leary S.C., Kaufman B.A., Pellecchia G., Guercin G.H., Mattman A., Jaksch M., and Shoubridge E.A. Human SCO1 and SCO2 have independent, cooperative functions in copper delivery to cytochrome c oxidase. Hum. Mol. Genet. 13 (2004) 1839-1848
20. Leary S.C., Mattman A., Wai T., Koehn D.C., Clarke L.A., Chan S., Lomax B., Eydoux P., Vallance H.D., and Shoubridge E.A. A hemizygous SCO2 mutation in an early onset rapidly progressive, fatal cardiomyopathy. Mol. Genet. Metab. 89 (2006) 129-133
21. Lee J., Prohaska J.R., and Thiele D.J. Essential role for mammalian copper transporter Ctr1 in copper homeostasis and embryonic development. Proc. Natl. Acad. Sci. USA 98 (2001) 6842-6847
22. Lee J., Pena M.M., Nose Y., and Thiele D.J. Biochemical characterization of the human copper transporter Ctr1. J. Biol. Chem. 277 (2002) 4380-4387
23. Mufti A.R., Burstein E., Csomos R.A., Graf P.C., Wilkinson J.C., Dick R.D., Challa M., Son J.K., Bratton S.B., Su G.L., et al. XIAP is a copper binding protein deregulated in Wilson's disease and other copper toxicosis disorders. Mol. Cell 21 (2006) 775-785
24. Nose Y., Kim B.E., and Thiele D.J. Ctr1 drives intestinal copper absorption and is essential for growth, iron metabolism, and neonatal cardiac function. Cell Metab. 4 (2006) 235-244
25. Papadopoulou L.C., Sue C.M., Davidson M.M., Tanji K., Nishino I., Sadlock J.E., Krishna S., Walker W., Selby J., Glerum D.M., et al. Fatal infantile cardioencephalomyopathy with COX deficiency and mutations in SCO2, a COX assembly gene. Nat. Genet. 23 (1999) 333-337
26. Pase L., Voskoboinik I., Greenough M., and Camakaris J. Copper stimulates trafficking of a distinct pool of the Menkes copper ATPase (ATP7A) to the plasma membrane and diverts it into a rapid recycling pool. Biochem. J. 378 (2004) 1031-1037
27. Petris M.J., Mercer J.F., Culvenor J.G., Lockhart P., Gleeson P.A., and Camakaris J. Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking. EMBO J. 15 (1996) 6084-6095
28. Petris M.J., Smith K., Lee J., and Thiele D.J. Copper-stimulated endocytosis and degradation of the human copper transporter, hCtr1. J. Biol. Chem. 278 (2003) 9639-9646
29. Prohaska J.R. Changes in tissue growth, concentrations of copper, iron, cytochrome oxidase and superoxide dismutase subsequent to dietary or genetic copper deficiency in mice. J. Nutr. 113 (1983) 2048-2058
30. Rae T.D., Schmidt P.J., Pufahl R.A., Culotta V.C., and O'Halloran T.V. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 284 (1999) 805-808
31. Rees E.M., and Thiele D.J. From aging to virulence: forging connections through the study of copper homeostasis in eukaryotic microorganisms. Curr. Opin. Microbiol. 7 (2004) 175-184
32. Sacconi S., Salviati L., Sue C.M., Shanske S., Davidson M.M., Bonilla E., Naini A.B., De Vivo D.C., and DiMauro S. Mutation screening in patients with isolated cytochrome c oxidase deficiency. Pediatr. Res. 53 (2003) 224-230
33. Salviati L., Hernandez-Rosa E., Walker W.F., Sacconi S., DiMauro S., Schon E.A., and Davidson M.M. Copper supplementation restores cytochrome c oxidase activity in cultured cells from patients with SCO2 mutations. Biochem. J. 363 (2002) 321-327
34. Stiburek L., Vesela K., Hansikova H., Pecina P., Tesarova M., Cerna L., Houstek J., and Zeman J. Tissue-specific cytochrome c oxidase assembly defects due to mutations in SCO2 and SURF1. Biochem. J. 392 (2005) 625-632
35. Tao T.Y., and Gitlin J.D. Hepatic copper metabolism: insights from genetic disease. Hepatology 37 (2003) 1241-1247
36. Valnot I., Osmond S., Gigarel N., Mehaye B., Amiel J., Cormier-Daire V., Munnich A., Bonnefont J.P., Rustin P., and Rotig A. Mutations of the SCO1 gene in mitochondrial cytochrome c oxidase deficiency with neonatal-onset hepatic failure and encephalopathy. Am. J. Hum. Genet. 67 (2000) 1104-1109
37. Vesela K., Hansikova H., Tesarova M., Martasek P., Elleder M., Houstek J., and Zeman J. Clinical, biochemical and molecular analyses of six patients with isolated cytochrome c oxidase deficiency due to mutations in the SCO2 gene. Acta Paediatr. 93 (2004) 1312-1317