The NAD(+)/Sirtuin Pathway Modulates Longevity through Activation of Mitochondrial UPR and FOXO Signaling

Cell. 2013 Jul 18;154(2):430-41. doi: 10.1016/j.cell.2013.06.016.

Abstract

NAD(+) is an important cofactor regulating metabolic homeostasis and a rate-limiting substrate for sirtuin deacylases. We show that NAD(+) levels are reduced in aged mice and Caenorhabditis elegans and that decreasing NAD(+) levels results in a further reduction in worm lifespan. Conversely, genetic or pharmacological restoration of NAD(+) prevents age-associated metabolic decline and promotes longevity in worms. These effects are dependent upon the protein deacetylase sir-2.1 and involve the induction of mitonuclear protein imbalance as well as activation of stress signaling via the mitochondrial unfolded protein response (UPR(mt)) and the nuclear translocation and activation of FOXO transcription factor DAF-16. Our data suggest that augmenting mitochondrial stress signaling through the modulation of NAD(+) levels may be a target to improve mitochondrial function and prevent or treat age-associated decline.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Aging
  • Animals
  • Caenorhabditis elegans / physiology
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism
  • Forkhead Transcription Factors / metabolism*
  • Hepatocytes / metabolism
  • Longevity*
  • Mice
  • Mitochondria / metabolism*
  • NAD / metabolism*
  • Poly(ADP-ribose) Polymerase Inhibitors
  • Reactive Oxygen Species / metabolism
  • Signal Transduction*
  • Sirtuin 1 / genetics
  • Sirtuin 1 / metabolism
  • Sirtuins / genetics
  • Sirtuins / metabolism
  • Transcription Factors / metabolism
  • Unfolded Protein Response*

Substances

  • Caenorhabditis elegans Proteins
  • Forkhead Transcription Factors
  • Poly(ADP-ribose) Polymerase Inhibitors
  • Reactive Oxygen Species
  • Transcription Factors
  • daf-16 protein, C elegans
  • NAD
  • SIR-2.1 protein, C elegans
  • Sirt1 protein, mouse
  • Sirtuin 1
  • Sirtuins