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- Title
Phosphorylation regulates SIRT1 function.
- Authors
Sasaki, Tsutomu; Maier, Bernhard; Koclega, Katarzyna D; Chruszcz, Maksymilian; Gluba, Wendy; Stukenberg, P Todd; Minor, Wladek; Scrable, Heidi
- Abstract
SIR2 is an NAD(+)-dependent deacetylase [1]-[3] implicated in the regulation of lifespan in species as diverse as yeast [4], worms [5], and flies [6]. We previously reported that the level of SIRT1, the mammalian homologue of SIR2 [7], [8], is coupled to the level of mitotic activity in cells both in vitro and in vivo[9]. Cells from long-lived mice maintained SIRT1 levels of young mice in tissues that undergo continuous cell replacement by proliferating stem cells. Changes in SIRT1 protein level were not associated with changes in mRNA level, suggesting that SIRT1 could be regulated post-transcriptionally. However, other than a recent report on sumoylation [10] and identification of SIRT1 as a nuclear phospho-protein by mass spectrometry [11], post-translational modifications of this important protein have not been reported.
- Publication
PloS one, 2008, Vol 3, Issue 12, pe4020
- ISSN
1932-6203
- Publication type
Journal Article
- DOI
10.1371/journal.pone.0004020