Letter abstract
Nature Cell Biology 9, 445 - 452 (2007)
Published online: 11 March 2007 | Corrected online: 16 October 2008 | doi:10.1038/ncb1556
There is a Corrigendum (November 2008) associated with this Letter.
Uncoupling proteins 2 and 3 are fundamental for mitochondrial Ca2+ uniport
Michael Trenker1,2, Roland Malli1,2, Ismene Fertschai1, Sanja Levak-Frank1 & Wolfgang F. Graier1,2
Mitochondrial Ca2+ uptake is crucial for the regulation of the rate of oxidative phosphorylation1, the modulation of spatio-temporal cytosolic Ca2+ signals2, 3, 4 and apoptosis5. Although the phenomenon of mitochondrial Ca2+ sequestration, its characteristics and physiological consequences have been convincingly reported6, 7, the actual protein(s) involved in this process are unknown. Here, we show that the uncoupling proteins 2 and 3 (UCP2 and UCP3) are essential for mitochondrial Ca2+ uptake. Using overexpression, knockdown (small interfering RNA) and mutagenesis experiments, we demonstrate that UCP2 and UCP3 are elementary for mitochondrial Ca2+ sequestration in response to cell stimulation under physiological conditions — observations supported by isolated liver mitochondria of Ucp2-/- mice lacking ruthenium red-sensitive Ca2+ uptake. Our results reveal a novel molecular function for UCP2 and UCP3, and may provide the molecular mechanism for their reported effects8, 9, 10. Moreover, the identification of proteins fundemental for mitochondrial Ca2+ uptake expands our knowledge of the physiological role for mitochondrial Ca2+ sequestration.
- Institute of Molecular Biology and Biochemistry, Centre of Molecular Medicine, Medical University of Graz, Harrachgasse 21/III, 8010 Graz, Austria.
- These authors contributed equally to this work.
Correspondence to: Wolfgang F. Graier1,2 e-mail: wolfgang.graier@meduni-graz.at
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