ArticleJournal of the American Chemical Society2017
HDAC8 Substrates Identified by Genetically Encoded Active Site Photocrosslinking.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Dissecting the epigenetic orchestra of HDAC isoforms in breast cancer development: a review.Medical oncology (Northwood, London, England) · 2024Review
- Discovery of a Highly Potent and Selective HDAC8 Degrader: Advancing the Functional Understanding and Therapeutic Potential of HDAC8.Journal of medicinal chemistry · 2024Article
- Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells.Nature communications · 2024Article
- Activity Guided Azide-methyllysine Photo-trapping for Substrate Profiling of Lysine Demethylases.Journal of the American Chemical Society · 2023Article
- Lysine Deacetylase Substrate Selectivity: Distinct Interaction Surfaces Drive Positive and Negative Selection for Residues Following Acetyllysine.Biochemistry · 2023Article
- Proteomics-based trapping with single or multiple inactive mutants reproducibly profiles histone deacetylase 1 substrates.Journal of proteomics · 2023Article
- Histone deacetylase 8 inhibition prevents the progression of peritoneal fibrosis by counteracting the epithelial-mesenchymal transition and blockade of M2 macrophage polarization.Frontiers in immunology · 2023Article
- Phage-assisted, active site-directed ligand evolution of a potent and selective histone deacetylase 8 inhibitor.Protein science : a publication of the Protein Society · 2022Article
- Pathological Role of HDAC8: Cancer and Beyond.Cells · 2022Review
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
- Critical review of non-histone human substrates of metal-dependent lysine deacetylases.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Review
- HDAC8 promotes the dissemination of breast cancer cells via AKT/GSK-3β/Snail signals.Oncogene · 2020Article
- Review
- Recent Advances in Chemical Biology Using Benzophenones and Diazirines as Radical Precursors.Molecules (Basel, Switzerland) · 2020Review
- Structure, mechanism, and inhibition of the zinc-dependent histone deacetylases.Current opinion in structural biology · 2019Review
- A Genetically Encoded, Phage-Displayed Cyclic-Peptide Library.Angewandte Chemie (International ed. in English) · 2019Review
- Preparation of a new construct of human histone deacetylase 8 for the crystallization of enzyme-inhibitor complexes.Methods in enzymology · 2019Article
- HDAC1 Substrate Profiling Using Proteomics-Based Substrate Trapping.ACS chemical biology · 2018Article
- The HDAC6/8/10 inhibitor TH34 induces DNA damage-mediated cell death in human high-grade neuroblastoma cell lines.Archives of toxicology · 2018Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The histone deacetylase family comprises 18 enzymes that catalyze deacetylation of acetylated lysine residues; however, the specificity and substrate profile of each isozyme remains largely unknown. Due to transient enzyme-substrate interactions, conventional co-immunoprecipitation methods frequently fail to identify enzyme-specific substrates. Additionally, compensatory mechanisms often limit the ability of knockdown or chemical inhibition studies to achieve significant fold changes observed by acetylation proteomics methods. Furthermore, measured alterations do not guarantee a direct link between enzyme and substrate. Here we present a chemical crosslinking strategy that incorporates a photoreactive, non-natural amino acid, p-benzoyl-l-phenylalanine, into various positions of the structurally characterized isozyme histone deacetylase 8 (HDAC8). After covalent capture, co-immunoprecipitation, and mass spectrometric analysis, we identified a subset of HDAC8 substrates from human cell lysates, which were further validated for catalytic turnover. Overall, this chemical crosslinking approach identified novel HDAC8-specific substrates with high catalytic efficiency, thus presenting a general strategy for unbiased deacetylase substrate discovery.
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Registered trials
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