Vitamin K2 is a mitochondrial electron carrier that rescues pink1 deficiency

Science

Volumn 336, Issue 6086, 2012, Pages 1306-1310

  Vos, Melissa ^a,b   Esposito, Giovanni ^a,b   Edirisinghe, Janaka N ^c   Vilain, Sven ^a,b   Haddad, Dominik M ^a,b   Slabbaert, Jan R ^a,b   Van Meensel, Stefanie ^a,b   Schaap, Onno ^a,b   De Strooper, Bart ^a,b   Meganathan, R ^c   Morais, Vanessa A ^a,b   Verstreken, Patrik ^a,b  

^a DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^b UNIVERSITY OF LEUVEN   (Belgium)

^c NORTHERN ILLINOIS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; FARNOQUINONE; UBIQUINONE; DROSOPHILA PROTEIN; HEIX PROTEIN, DROSOPHILA; PARKIN PROTEIN, DROSOPHILA; PINK1 PROTEIN, DROSOPHILA; PROTEIN SERINE THREONINE KINASE; UBIQUITIN PROTEIN LIGASE;

BIOCHEMISTRY; BLOOD; COAGULATION; ELECTRON; FLY; GENE EXPRESSION; MITOCHONDRION; MUTATION; VITAMIN;

ARTICLE; CONTROLLED STUDY; DISORDERS OF MITOCHONDRIAL FUNCTIONS; DROSOPHILA; DRUG MECHANISM; GENE; GENE MUTATION; GENETIC ASSOCIATION; MITOCHONDRIAL ENERGY TRANSFER; NONHUMAN; PARKINSON DISEASE; PINK1 GENE; PRIORITY JOURNAL; ANIMAL; ELECTRON TRANSPORT; ESCHERICHIA COLI; FLYING; GENETICS; METABOLISM; MITOCHONDRIAL MEMBRANE POTENTIAL; MITOCHONDRION; MUSCLE MITOCHONDRION; MUTATION; OXYGEN CONSUMPTION; ULTRASTRUCTURE;

EUKARYOTA;

ADENOSINE TRIPHOSPHATE; ANIMALS; DROSOPHILA; DROSOPHILA PROTEINS; ELECTRON TRANSPORT; ESCHERICHIA COLI; FLIGHT, ANIMAL; GENES, INSECT; MEMBRANE POTENTIAL, MITOCHONDRIAL; MITOCHONDRIA; MITOCHONDRIA, MUSCLE; MUTATION; OXYGEN CONSUMPTION; PROTEIN-SERINE-THREONINE KINASES; UBIQUINONE; UBIQUITIN-PROTEIN LIGASES; VITAMIN K 2;

EID: 84861983560     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1218632     Document Type: Article

References (26)

1. M. Vila, S. Przedborski, Nat. Med. 10 (suppl.), S58 (2004).
2. W. Mandemakers, V. A. Morais, B. De Strooper, J. Cell Sci. 120, 1707 (2007).
3. E. M. Valente et al., Science 304, 1158 (2004); 10.1126/science.1096284.
4. I. E. Clark et al., Nature 441, 1162 (2006).
5. J. Park et al., Nature 441, 1157 (2006).
6. V. A. Morais et al., EMBO Mol. Med. 1, 99 (2009).
7. P. Verstreken et al., Neuron 63, 203 (2009).
8. P. R. Hiesinger et al., Cell 121, 607 (2005).
9. V. Uytterhoeven, S. Kuenen, J. Kasprowicz, K. Miskiewicz, P. Verstreken, Cell 145, 117 (2011).
10. Materials and methods are available as supplementary materials on Science Online.
11. S. Vilain et al., PLoS Genet. 8, e1002456 (2012).
12. K. Suvarna, D. Stevenson, R. Meganathan, M. E. S. Hudspeth, J. Bacteriol. 180, 2782 (1998).
13. K. Nakagawa et al., Nature 468, 117 (2010).
14. J. M. Conly, K. Stein, L. Worobetz, S. Rutledge-Harding, Am. J. Gastroenterol. 89, 915 (1994).
15. H. Deng, M. W. Dodson, H. Huang, M. Guo, Proc. Natl. Acad. Sci. U.S.A. 105, 14503 (2008).
16. E. C. C. Lin, D. Kuritzkes, in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, F. C. Neidhardt et al., Eds. (American Society for Microbiology, Washington, DC, 1987), pp. 202-221.
17. M. L. Nickerson et al., PLoS ONE 5, e10760 (2010).
18. H. H. Thijssen, M. J. Drittij-Reijnders, Br. J. Nutr. 72, 415 (1994).
19. Y. Usui et al., J. Chromatogr. 489, 291 (1989).
20. B. de Paepe et al., Pediatr. Res. 59, 2 (2006).
21. S. L. Hebert, I. R. Lanza, K. S. Nair, Mech. Ageing Dev. 131, 451 (2010).
22. A. Orr et al., PLoS ONE 2, e685 (2007).
23. V. S. Yellore et al., Mol. Vis. 13, 1777 (2007).
24. J. S. Weiss et al., Invest. Ophthalmol. Vis. Sci. 48, 5007 (2007).
25. A. Garner, R. C. Tripathi, Br. J. Ophthalmol. 56, 400 (1972).
26. S. McCarthy, M. Somayajulu, M. Sikorska, H. Borowy-Borowski, S. Pandey, Toxicol. Appl. Pharmacol. 201, 21 (2004).