ArticleThe Journal of biological chemistry2025
Structural and enzymatic plasticity of SIRT6 deacylase activity.
Article in The Journal of biological chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Lysine l-Lactylation: Bridging Metabolism, Chromatin and Disease.Cell proliferation · 2026Review
- Mechanistic and functional integration of sirtuin deacylases: from substrate specificity to biological outcomes.Glycoconjugate journal · 2026Review
- Histone modification cross-talk: analytical tools and molecular mechanisms.The Biochemical journal · 2026Review
- Role of Sirtuin 6 in the Pathogenesis of Metabolic Dysfunction-Associated Steatotic Liver Disease.Current issues in molecular biology · 2026Review
- Processes and therapeutic perspectives of acylation modifications of lysine and cysteine in tumors.Cell communication and signaling : CCS · 2026Review
- Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026Review
- Kinetic Analysis of HDAC- and Sirtuin-Mediated Deacylation on Chemically Defined Histones and Nucleosomes.Current protocols · 2025Article
- Lactylation Modification and Aging: A Molecular Link in the Life Process.Aging and disease · 2025Review
- From ketogenic metabolism to targeted therapeutics: current advances in β-hydroxybutyrylation.Frontiers in immunology · 2025Review
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Sirtuin 6 (SIRT6) is an NAD-dependent protein deacylase that targets lysine residues in histones in the cell nucleus, where it helps maintain genome stability and links metabolism to epigenetic control. Dysregulation of SIRT6 is believed to be associated with aging and cancer, making it of pharmacological interest. In this study, we use cryo-EM and enzymology to explore SIRT6 preference and adaptability toward different nucleosomal substrates. We have visualized a trapped complex of SIRT6 in the process of deacylating H3K27, demonstrating how SIRT6 undergoes conformational changes to remove differently positioned histone marks. Additional biochemical studies further reveal the plasticity of SIRT6, which accommodates various metabolism-linked modifications, such as lysine lactylation and β-hydroxybutyrylation. To further understand the basis for substrate selectivity of SIRT6, we explore the effects of an established G60A enzyme mutation, proximal H3 modifications, and small-molecule modulators. These findings highlight the versatility of SIRT6 and provide key mechanistic insights into its molecular recognition.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.