Protein deacetylation by SIRT1

An emerging key post-translational modification in metabolic regulation

Jiujiu Yu, Johan Auwerx

Research output: Contribution to journalReview article

71 Citations (Scopus)

Abstract

The biological function of most proteins relies on reversible post-translational modifications, among which phosphorylation is most prominently studied and well recognized. Recently, a growing amount of evidence indicates that acetylation-deacetylation reactions, when applied to crucial mediators, can also robustly affect the function of target proteins and thereby have wide-ranging physiological impacts. Sirtuin 1 (SIRT1), which functions as a nicotinamide adenine dinucleotide (NAD+)-dependent protein deacetylase, deacetylates a wide variety of metabolic molecules in response to the cellular energy and redox status and as such causes significant changes in metabolic homeostasis. This review surveys the evidence for the emerging role of SIRT1-mediated deacetylation in the control of metabolic homeostasis.

Original languageEnglish (US)
Pages (from-to)35-41
Number of pages7
JournalPharmacological Research
Volume62
Issue number1
DOIs
StatePublished - Jul 1 2010

Fingerprint

Sirtuin 1
Post Translational Protein Processing
NAD
Homeostasis
Proteins
Acetylation
Oxidation-Reduction
Phosphorylation

Keywords

  • Deacetylation
  • Metabolic homeostasis
  • NAD
  • SIRT1

ASJC Scopus subject areas

  • Pharmacology

Cite this

Protein deacetylation by SIRT1 : An emerging key post-translational modification in metabolic regulation. / Yu, Jiujiu; Auwerx, Johan.

In: Pharmacological Research, Vol. 62, No. 1, 01.07.2010, p. 35-41.

Research output: Contribution to journalReview article

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