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Our data provide strong evidence that sirtuin-2 controls the functional ability of the autophagic system through acetylation and highlight the association between mitochondrial metabolism and neurodegeneration in sporadic Parkinson's disease.
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Data found that SIRT2 is a novel deacetylase of HSP90, enhances its ubiquitination-mediated proteasomal degradation, and consequently down-regulates HSP90/LIMK1/cofilin-linked actin polymerization regulation pathway. The deacetylase activity of SIRT2 is required to reduce cell motility by regulating the stability of HSP90. These results demonstrate that SIRT2 functions as a tumor suppressor.
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we provide insight into the regulation of SIRT2 on gastric cancer metabolism and metastasis. SIRT2 increased PEPCK1 protein levels and mitochondrial activity, as well as induced cell migration and invasion by activating the RAS/ERK/JNK/MMP-9 pathway
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MiR150 plays an important role in the development of lung cancer by serving as an oncogene via the SIRT2/JMJD2A signaling pathway.
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Studied association of SIRT2 and p53/NF-kB p65 signal pathways in preventing high glucose-induced vascular endothelial cell injury. Results demonstrated that SIRT2 overexpression is associated with deacetylation of p53 and NF-kB p65, which inhibits the high glucose induced apoptosis and vascular endothelial cell inflammation response.
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The authors report that one of the K-Ras splice variants, K-Ras4a, is subject to lysine fatty acylation, a previously under-studied protein post-translational modification. Sirtuin 2 (SIRT2), one of the mammalian nicotinamide adenine dinucleotide (NAD)-dependent lysine deacylases, catalyzes the removal of fatty acylation from K-Ras4a.
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Low SIRT2 expression is associated with recurrence in prostate cancer.
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SIRT2 participates in the activation of fibroblasts and tubulointerstitial fibrosis, which is mediated via regulation of the MDM2 pathway, and the downregulation of SIRT2.
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Findings suggested that the DNA sequence variants may increase SIRT2 gene promoter activity and SIRT2 levels, contributing to T2D development as a risk factor.
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Chemical inhibitors against SIRT2 suppress G6PD activity, leading to reduced cell proliferation of leukaemia cells, but not normal hematopoietic stem and progenitor cells. Importantly, SIRT2 is overexpressed in clinical acute myeloid leukaemia samples, while K403 acetylation is downregulated and G6PD catalytic activity is increased comparing to that of normal control.
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SIRT2 may have a role in unfavorable prognosis of acute myeloid leukemia
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Data suggest that inhibition of sirtuin 1 and sirtuin 2 in hepatocellular carcinoma cells (a) impairs cell survival and cell migration and (b) down-regulates expression of P-glycoprotein and MRP3 (ATP binding cassette subfamily C member 3).
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SIRT2 inhibition may improve microtubule assembly thus representing a valid approach as disease-modifying therapy for Alzheimer's disease.
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Data show that single nucleotide polymorphism rs2015C in sirtuin 2 protein (SIRT2) gene 3'-UTR was significantly associated with increased risk of colorectal cancer (CRC).
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Authors show that SIRT2 is downregulated in insulin-resistant hepatocytes and livers, and this was accompanied by increased generation of reactive oxygen species, activation of stress-sensitive ERK1/2 kinase, and mitochondrial dysfunction.
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Those findings highlight the potential role of SIRT2 in HBV and HBV-mediated HCC by interaction with HBx.
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The SIRT2 functions as a mitochondrial sirtuin, as well as a regulator of autophagy/mitophagy to maintain mitochondrial biology, thus facilitating cell survival.
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increased expression of SRF that was observed in the aged heart may affect SIRT2 gene expression and contribute to altered metabolic status in senescence
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SIRT2 and RIPK1 were localized to the syncytiotrophoblast, villous leukocytes and vasculature in all preterm placentas. A significant reduction in SIRT2 protein expression in both preeclampsia and fetal growth restricted placentas was identified. Immunofluorescence identified both SIRT2 and RIPK1 in the cytotrophoblast cytoplasm.
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mutations in sirtuin2 increase the stability of the conserved catalytic sirtuin domain, thereby increasing the catalytic efficiency of the mutant enzymes.
