Sirtuin 2 Regulates Protein LactoylLys Modifications
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Summary
Using chemical biology and CRISPR‐Cas9, it is shown that SIRT2 controls the abundance of this PTM both globally and on chromatin, addressing a major gap in the understanding of how nonenzymatic PTMs are regulated and controlled.
- Type
- article
- Published
- 2021-03-16
- Cited by
- 70
- References
- 29
- Access
- Open access
- OpenAlex
- https://openalex.org/W3139135627
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:232263377
Keywords
Sirtuin, SIRT2, CRISPR, Mechanism (biology), Function (biology)
References
- One-Carbon Metabolism in Health and Disease
- Emerging Role of Sirtuin 2 in the Regulation of Mammalian Metabolism.
- Small Changes Huge Impact: The Role of Protein Posttranslational Modifications in Cellular Homeostasis and Disease
- Functional lysine modification by an intrinsically reactive primary glycolytic metabolite
- Sirtuins as regulators of metabolism and healthspan
- SIRT2 regulates NF-κB-dependent gene expression through deacetylation of p65 Lys310
- Sirtuins: Sir2-related NAD-dependent protein deacetylases
- SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis.
- Sirtuins Link Inflammation and Metabolism
- Stable Histone Adduction by 4-Oxo-2-nonenal: A Potential Link between Oxidative Stress and Epigenetics
- SIRT2 Reverses 4-Oxononanoyl Lysine Modification on Histones
- Non-enzymatic N-acetylation of Lysine Residues by AcetylCoA Often Occurs via a Proximal S-acetylated Thiol Intermediate Sensitive to Glyoxalase II
- NF-κB signaling in inflammation
- Nuclear sirtuins and inflammatory signaling pathways.
- LC–MS/MS-based quantitative study of the acyl group- and site-selectivity of human sirtuins to acylated nucleosomes
- Regulation of chromatin and gene expression by metabolic enzymes and metabolites
- Lysine benzoylation is a histone mark regulated by SIRT2
- Methylglyoxal-derived posttranslational arginine modifications are abundant histone marks
- Profiling of Methylglyoxal Blood Metabolism and Advanced Glycation End-Product Proteome Using a Chemical Probe.
- Prediction of Hemolytic Toxicity for Saponins by Machine-Learning Methods.
Cited by
- Biochemical genesis of enzymatic and non-enzymatic post-translational modifications
- Class I histone deacetylases (HDAC1–3) are histone lysine delactylases
- Chiral Posttranslational Modification to Lysine ε-Amino Groups.
- SIRT2 functions as a histone delactylase and inhibits the proliferation and migration of neuroblastoma cells
- Uncovering Robust Delactoylase and Depyruvoylase Activities of HDAC Isoforms.
- Biochemical Mechanisms of Sirtuin-Directed Protein Acylation in Hepatic Pathologies of Mitochondrial Dysfunction
- Small Changes Make the Difference for SIRT2: Two Different Binding Modes for 3-Arylmercapto-Acylated Lysine Derivatives.
- The role and mechanism of histone lactylation in health and diseases
- Lactylation, an emerging hallmark of metabolic reprogramming: Current progress and open challenges
- Methylglyoxal and Its Adducts: Induction, Repair, and Association with Disease
- Biosynthesis of D/L-lactate from methylglyoxal
- Lactate and Lactylation in the Brain: Current Progress and Perspectives
- Lactate‐induced protein lactylation: A bridge between epigenetics and metabolic reprogramming in cancer
- New Histone Lysine Acylation Biomarkers and Their Roles in Epigenetic Regulation
- A global view of the human post-translational modification landscape
- Epigenetic meets metabolism: novel vulnerabilities to fight cancer
- Lactoylglutathione promotes inflammatory signaling in macrophages
- Effects of Dimerization on the Deacylase Activities of Human SIRT2
- Lactoylglutathione promotes inflammatory signaling in macrophages through histone lactoylation
- A pan-cancer multi-omics analysis of lactylation genes associated with tumor microenvironment and cancer development
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