Human SIR2 deacetylates p53 and antagonizes PML/p53‐induced cellular senescence

By E. Langley, M. Pearson, M. Faretta, U. Bauer, Roy A. Frye, S. Minucci, Pier Giuseppe Pelicci, Tony Kouzarides. EMBO Journal, 2002

916 citations recorded by the source corpus.

Subfields: Geriatrics and Gerontology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/ed77301f9cad87a6129bf20df5d177dcd9f4f241

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Geriatrics and Gerontology

1. D. Sinclair
2. Johan Auwerx
3. E. Verdin
4. L. Guarente
5. C. Cantó
6. Joseph A. Baur
7. Brian K. Kennedy
8. V. Longo

In Molecular Biology

1. L. Guarente
2. W. Gu
3. E. Verdin
4. D. Sinclair
5. Johan Auwerx
6. C. Brooks
7. R. Mostoslavsky
8. Brian J. North

Citations in the corpus

• Sirtuins in aging and age-related disease. (2006, background): “Whereas Sirt1 activity was originally reported to inhibit apoptosis through deacetylation of p53 (Langley et al., 2002; Luo et al., 2001), more recent reports suggest that although Sirt1 can deacetylate p53 there is little effect on p53-mediated biological outcomes (Kamel et al.”
• Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ (2004, neutral): “Antibodies used were anti-Sirt1 ( Upstate ), anti-NCoR ( Upstate ), anti-PPAR-γ ( SantaCruz ), anti-C/EBP-α ( SantaCruz ) and anti-Sirt1 antiseru”
• SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis (2007, methodology): “Third, this increase is accompanied by an increase in the acetylation status of lysine 382 of p53 (Figure 5B), a modification known to stabilize p53 and potentiate its apoptotic function (Luo et al, 2001; Vaziri et al, 2001; Langley et al, 2002).”
• SIRTUIN 1 AND SIRTUIN 3: PHYSIOLOGICAL MODULATORS OF METABOLISM (2012, background): “As SIRT1 binds and deacetylates p53 to decrease its transcriptional activity, p53 is suggested to play a central role in SIRT1-mediated functions in tumorigenesis and senescence (78, 189, 208, 339).”
• The Mammalian SIR2α Protein Has a Role in Embryogenesis and Gametogenesis (2003, background): “In fact, there is evidence from transfection experiments suggesting that p53 is a substrate for SIR2 and that deacetylation of p53 downregulates its transactivation function (25, 29, 50).”
• Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. (2003, background): “Sir2a co-localizes in promyelocytic leukemia (PML) nuclear bodies with p53 [77 ], and was shown to undergo a conformational change when bound to acetylated p53 [78].”
• Awakening guardian angels: drugging the p53 pathway (2009, background): “p53 deacetylation by SIRT1 impairs p53 stability and transcriptional activit”
• Calorie restriction--the SIR2 connection. (2005, background): “The first example of this was p53, which was shown to be deacetylated and downregulated by Sirt1 (Luo et al., 2001; Vaziri et al., 2001; Langley et al., 2002).”
• Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase (2004, background): “SIRT1 activity provides a cell survival advantage following DNA damage, in part, by deacetylating lysine 382 on the p53 tumor suppressor protein in vitro and in vivo (Luo et al, 2001; Vaziri et al, 2001; Langley et al, 2002;”
• Resveratrol as an anti-inflammatory and anti-aging agent: mechanisms and clinical implications. (2005, background): “Deacetylation of this residue by SIR1 decreases the activity and half-life of p53, and increases cell survival under a variety of DNA damaging conditions [97–99].”