anti-Sirtuin 2 (SIRT2) Antibodies

Fruit Fly (Drosophila melanogaster) Sirtuin 2 (SIRT2) interaction partners

1. Sirt2 has an role in the regulation of mitochondrial energy metabolism.

Arabidopsis thaliana Sirtuin 2 (SIRT2) interaction partners

1. This work establishes a mechanism by which histone deacetylases SRT1 and SRT2 interact with ENAP1 to mediate transcriptional repression by regulating the levels of histone H3 lysine 9 acetylation in the ethylene signaling

2. SRT2 is important in fine-tuning mitochondrial energy metabolism.

3. AtSRT2 is a deacetylase that negatively regulates the plant basal defense and PR1 expression.

Human Sirtuin 2 (SIRT2) interaction partners

1. SIRT2-mediated inactivation of p73 is critical for the proliferation and tumorigenicity of glioblastoma cells.

2. Here, the authors report that GSK3alpha and GSK3beta are acetylated at Lys246 and Lys183, respectively. They found that SIRT2 deacetylates GSK3beta, and thus enhances its binding to ATP.

3. SIRT2-C/T-EMs are the best responders. Some Sirtuin modulators might be potential candidates for AD treatment.

4. SIRT2 gene expression is altered in adipose tissue from overweight and obese subjects compared to normal weight subjects.

5. SIRT1 and SIRT2 expression and AMPK levels decrease in children with obesity and insulin resistance (IR); targeting SIRT1 can be valuable in preventing obesity-associated IR in childhood and adolescence

6. miR-486-3p binds to the 3' UTR of SIRT2 and influences the translation of SIRT2.

7. Study discovered that histone lysine benzoylation (Kbz) marks are associated with gene expression and have physiological relevance distinct from histone acetylation and demonstrated that SIRT2, a NAD+-dependent protein deacetylase, removes histone Kbz both in vitro and in vivo.

8. 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.

9. 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.

10. 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

11. MiR150 plays an important role in the development of lung cancer by serving as an oncogene via the SIRT2/JMJD2A signaling pathway.

12. 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.

13. 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.

14. Low SIRT2 expression is associated with recurrence in prostate cancer.

15. SIRT2 participates in the activation of fibroblasts and tubulointerstitial fibrosis, which is mediated via regulation of the MDM2 pathway, and the downregulation of SIRT2.

16. Findings suggested that the DNA sequence variants may increase SIRT2 gene promoter activity and SIRT2 levels, contributing to T2D development as a risk factor.

17. 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.

18. SIRT2 may have a role in unfavorable prognosis of acute myeloid leukemia

19. 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).

20. SIRT2 inhibition may improve microtubule assembly thus representing a valid approach as disease-modifying therapy for Alzheimer's disease.

Cow (Bovine) Sirtuin 2 (SIRT2) interaction partners

1. These results provide insights into the potential mechanisms by which SIRT2-dependent deacetylation activity exerts its effects on oocyte quality.

2. the data support the hypothesis that SIRT2 regulates steroid hormone synthesis via the Peroxisome Proliferator-Activated Receptors/Liver X Receptor-alpha pathways in ovarian granulosa cells.

3. the novel 12-bp indel of SIRT1 gene, the 7-bp indel of SIRT2 gene and the 26-bp indel of SIRT3 gene were firstly reported, respectively. The association analysis indicated that the indels within SIRT1 and SIRT2 genes were significantly associated with body measurement traits such as body weight, chest circumference, height at hip cross, hip width, body height, etc.

4. The results indicate that the variations in the class I sirtuin genes and their corresponding genotypes may be considered as molecular markers for economic traits in cattle breeding.

5. An association analysis showed that the two loci of SIRT2 were significantly correlated with some body size traits and the H2H2 (-CT-CT-) diplotypes performed better than other combinations.

6. Data suggest that the silent information regulator 2 (SIRT2) gene may be a candidate gene for marker-assisted selection in the development of breeding programs for Qinchuan cattle.

Mouse (Murine) Sirtuin 2 (SIRT2) interaction partners

1. that Sirt2-dependent BubR1 deacetylation involves in the regulation of meiotic apparatus in normal oocytes and mediates the effects of advanced maternal age on oocyte quality

2. Direct oxidation modulates SIRT2 function during hyper-inflammatory phase of obesity with sepsis via redox sensitive cysteines.

3. SIRT2 plays a critical role in mediating the radiation-induced DNA damage response, thus regulating radiation-induced cell death and survival

4. Study indicates that Sirtuin2 (SIRT2) enhances the tumoricidal activity of liver NK cells in hepatocellular carcinoma (HCC).

5. SIRT2 was up-regulated during neuronal ischemia and translocated into neuronal nuclei.

6. SIRT2 deacetylates cyclin-dependent kinase 9 (CDK9) in a type I IFN-dependent manner and that the CDK9 deacetylation is essential for STAT1 phosphorylation at Ser-727.

7. Study in mice reports that Marcks is regulated by acetylation through Tip60 and Sirt2. Maternal diabetes-induced MARCKS acetylation is required for its phosphorylation, which disables the protective effects of MARCKS on mitochondria and the endoplasmic reticulum, leading to cellular organelle stress and neural tube defect formation.

8. Study discovered that histone lysine benzoylation (Kbz) marks are associated with gene expression and have physiological relevance distinct from histone acetylation and demonstrated that SIRT2, a NAD+-dependent protein deacetylase, removes histone Kbz both in vitro and in vivo.

9. These findings indicate that the NAD(+)/SIRT2 pathway is an important mediator through which silybin prevents NLRP3 inflammasome activation during NAFLD

10. both NAD and NADH significantly increased the intracellular ATP levels of BV2 microglia, which were attenuated by SIRT2 siRNA, the SIRT2 inhibitor AGK2, and the phosphatidylinositol 3-kinase/Akt inhibitor LY294002. Results suggested that SIRT2 mediates the NAD-induced and NADH-induced increase in Akt phosphorylation in BV2 microglia.

11. These findings suggest that SIRT2 inhibited atherosclerotic plaque progression and enhanced plaque stability in LDL receptor knockout mice by inhibiting macrophage polarization towards the M1 phenotype.

12. Results provide a novel link between SIRT2 and physiological aging impacting the axonal compartment of the central nervous system, while supporting a major role for SIRT2 in orchestrating its metabolic regulation.

13. CDK5-mediated phosphorylation of Sirt2 has a role in to depressive-like behavior induced by social defeat stress

14. These results confirm that SIRT2 inhibition is able to reverse anhedonia in different animal models and highlight the need to further investigate the role of SIRT2 inhibitors as new antidepressant agents.

15. SIRT2 knockout mice show marked up-regulation in AMPAR acetylation and protein accumulation, aberrant synaptic plasticity and impaired memory.

16. SIRT2 inhibition may improve microtubule assembly thus representing a valid approach as disease-modifying therapy for Alzheimer's disease.

17. 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.

18. Given the significance of KRAS activity as a driver in tumorigenesis, identification of K147 acetylation as a novel post-translational modification directed by SIRT2 in vivo may provide a better understanding of the mechanistic link regarding the crosstalk between non-genetic and genetic factors in KRAS driven tumors.

19. SIRT2 modulates microvascular inflammation in sepsis and affects survival

20. This study showed that Sirt2-dependent GKRP deacetylation improves impaired HGU and suggest that it may be a therapeutic target for type 2 diabetes.