Gene interactions and pathways from curated databases and text-mining

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SIRT1 — TP53

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Vaziri et al., Cell 2001 : Expression of wild-type hSir2 in human cells reduces the transcriptional activity of p53
Ford et al., Cancer Res 2005 : Combined gene knockout with RNAi cosilencing experiments indicate that SIRT1 and Bcl-2 may suppress separable apoptotic pathways in the same cell lineage and that the SIRT1 regulated pathway is independent of p53 , Bax, and caspase-2
Kamel et al., Aging Cell 2006 : Upon re-examination of the role of SirT1 in modulating p53 activity, we found that while SirT1 interacts with p53, the SirT1 protein had little effect on p53 dependent transcription of transfected or endogenous genes and did not affect the sensitivity of thymocytes and splenocytes to radiation induced apoptosis
Xi et al., Acta Pharmacol Sin 2008 : Importantly, the inhibition of SIRT1 contributed to the activation of p53 and the inactivation of the PI3-K/Akt signaling pathway increased the expression of the p53 protein and downregulated the SIRT1 protein expression
Han et al., Cell stem cell 2008 : SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization ... Although SIRT1, a p53 deacetylase, inhibits p53 mediated transactivation, how SIRT1 regulates these p53 multifunctions is unclear
Yamakuchi et al., Proc Natl Acad Sci U S A 2008 : MiR-34 inhibition of SIRT1 leads to an increase in acetylated p53 and expression of p21 and PUMA, transcriptional targets of p53 that regulate the cell cycle and apoptosis, respectively
Pediconi et al., Mol Cell Biol 2009 : The NAD ( + ) -dependent histone deacetylase hSirT1 regulates cell survival and stress responses by inhibiting p53- , NF-kappaB-, and E2F1 dependent transcription
Jung-Hynes et al., Cell cycle (Georgetown, Tex.) 2009 (Prostatic Neoplasms) : Since p53 is a target for deacetylation by Sirt1, we wanted to determine the involvement of p53 in Sirt1 inhibition mediated responses in PCa
van Leeuwen et al., Adv Cancer Res 2009 (Neoplasms) : Preliminary observations also suggest that sirtuin mediated modulation of p53 can also take place indirectly through changes in cellular processes ( e.g., nucleolar function and p300 activity ) known to affect p53
Gagarina et al., Arthritis Rheum 2010 (Osteoarthritis) : Expression of SirT1 in chondrocytes led to activation of IGFR and the downstream kinases phosphatidylinositol 3-kinase, phosphoinosite dependent protein kinase 1, mTOR, and Akt, which in turn phosphorylated MDM2, inhibited p53 , and blocked apoptosis
Lynch et al., PloS one 2010 : Thus, SIRT1 mediated inhibition of p53 has been identified as a key node in the common biology of cancer, metabolism, development and ageing ... We also identify an auto-regulatory loop whereby SIRT1-dExon8 can regulate p53 , while in reciprocal p53 can influence SIRT1 splice variation
Seo et al., Neurobiol Aging 2012 : Resveratrol mediated SIRT1 activation decreased the acetylation of p53 and p65 induced by prion protein and SIRT1 inhibitor
Liu et al., Proc Natl Acad Sci U S A 2011 : Methyltransferase Set7/9 regulates p53 activity by interacting with Sirtuin 1 (SIRT1)
Rodella et al., Age (Dordrecht, Netherlands) 2013 (Atherosclerosis...) : We demonstrate that SIRT1 and eNOS decresed in APOE mice between 6 and 15 weeks and that aging induced an elevated expression of p53 and ET-1 in APOE animals
Dixit et al., Cell death & disease 2012 (Brain Neoplasms...) : This ability of CK2-Is to sensitize glioma to TNFa induced death via multiple mechanisms involving abrogation of NF-?B activation, reactivation of wild-type p53 function and SIRT1 inhibition warrants investigation
Li et al., Cancer Cell 2012 (Leukemia, Myelogenous, Chronic, BCR-ABL Positive) : Activation of p53 by SIRT1 inhibition enhances elimination of CML leukemia stem cells in combination with imatinib ... Activation of p53 via SIRT1 inhibition represents a potential approach to target CML LSC
Xie et al., Cancer Sci 2012 (Carcinoma, Hepatocellular...) : The current findings indicate that SirT1 confers a higher radioresistance in hypoxic cells than in normoxic cells due to the decreased levels of c-Myc protein and its acetylation, and that a c-Myc dependent radiation induced phosphorylated p53 may be involved
Busch et al., J Biol Chem 2012 (Tendinopathy) : Overall, these results suggest for the first time that Sirt-1 can regulate p53 and NF-?B signaling via deacetylation, demonstrating a novel role for resveratrol in the treatment of tendinitis/tendinopathy
Castro et al., J Hepatol 2013 (Fatty Liver...) : Finally, p53 overexpression activated miR-34a/SIRT1/p53 , which in turn was inhibited by UDCA, via decreased p53 transcriptional activity
van Leeuwen et al., Mol Cancer Ther 2013 : These results help understand why inhibition of both SirT1 and SirT2 is needed to achieve effective activation of p53 by small-molecule sirtuin inhibitors
Adlakha et al., Cell death & disease 2013 : miR-128 inhibition of SIRT1 led to an increase in acetylated p53 and its transcriptional targets