Science. 2012 May 14. [Epub ahead of print]
Vos M, Esposito G, Edirisinghe JN, Vilain S, Haddad DM, Slabbaert JR, Van Meensel S, Schaap O, De Strooper B, Meganathan R, Morais VA, Verstreken P.
Abstract
Human
UBIAD1 localizes to mitochondria and converts vitamin K(1) to vitamin
K(2). Vitamin K(2) is best known as a cofactor in blood coagulation,
but in bacteria it is a membrane-bound electron carrier. Whether
vitamin K(2) exerts a similar carrier function in eukaryotic cells is
unknown. We identified Drosophila UBIAD1/Heix as a modifier of pink1, a
gene mutated in Parkinson's disease that affects mitochondrial
function. Here, we found that vitamin K(2) was necessary and sufficient
to transfer electrons in Drosophila mitochondria. Heix mutants showed
severe mitochondrial defects that were rescued by vitamin K(2), and,
similar to ubiquinone, vitamin K(2) transferred electrons in Drosophila
mitochondria, resulting in more efficient adenosine triphosphate (ATP)
production. Thus, mitochondrial dysfunction was rescued by vitamin K(2)
that serves as a mitochondrial electron carrier, helping to maintain
normal ATP production.
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