@article{3946,
  keywords = {Animals, Mice, Biological Transport, Humans, Cell Line, Genetic Complementation Test, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Mitochondria, NAD, Mitochondrial Proteins, Cell Respiration, Nucleotide Transport Proteins, Organic Cation Transport Proteins},
  author = {Timothy Luongo and Jared Eller and Mu-Jie Lu and Marc Niere and Fabio Raith and Caroline Perry and Marc Bornstein and Paul Oliphint and Lin Wang and Melanie McReynolds and Marie Migaud and Joshua Rabinowitz and F Brad Johnson and Kai Johnsson and Mathias Ziegler and Xiaolu Cambronne and Joseph Baur},
  title = {SLC25A51 is a mammalian mitochondrial NAD transporter.},
  abstract = { <p>Mitochondria require nicotinamide adenine dinucleotide (NAD) to carry out the fundamental processes that fuel respiration and mediate cellular energy transduction. Mitochondrial NAD transporters have been identified in yeast and plants, but their existence in mammals remains controversial. Here we demonstrate that mammalian mitochondria can take up intact NAD,~and identify SLC25A51 (also known as MCART1)-an essential mitochondrial protein of previously unknown function-as a mammalian mitochondrial NAD transporter. Loss of SLC25A51 decreases mitochondrial-but not whole-cell-NAD content, impairs mitochondrial respiration, and blocks the uptake of NAD into isolated mitochondria. Conversely, overexpression of SLC25A51 or SLC25A52 (a nearly identical paralogue of SLC25A51) increases mitochondrial NAD levels and restores NAD uptake into yeast mitochondria lacking endogenous NAD transporters. Together, these findings identify SLC25A51 as a mammalian transporter capable of importing NAD into mitochondria.</p> },
  year = {2020},
  journal = {Nature},
  volume = {588},
  pages = {174-179},
  month = {2020 Dec},
  issn = {1476-4687},
  doi = {10.1038/s41586-020-2741-7},
  language = {eng},
}