The many lives of KATs - detectors, integrators and modulators of the cellular environment
- PMID: 30390049
- DOI: 10.1038/s41576-018-0072-4
The many lives of KATs - detectors, integrators and modulators of the cellular environment
Abstract
Research over the past three decades has firmly established lysine acetyltransferases (KATs) as central players in regulating transcription. Recent advances in genomic sequencing, metabolomics, animal models and mass spectrometry technologies have uncovered unexpected new roles for KATs at the nexus between the environment and transcriptional regulation. Thousands of reversible acetylation sites have been mapped in the proteome that respond dynamically to the cellular milieu and maintain major processes such as metabolism, autophagy and stress response. Concurrently, researchers are continuously uncovering how deregulation of KAT activity drives disease, including cancer and developmental syndromes characterized by severe intellectual disability. These novel findings are reshaping our view of KATs away from mere modulators of chromatin to detectors of the cellular environment and integrators of diverse signalling pathways with the ability to modify cellular phenotype.
Similar articles
-
Identification of Novel Protein Lysine Acetyltransferases in Escherichia coli.mBio. 2018 Oct 23;9(5):e01905-18. doi: 10.1128/mBio.01905-18. mBio. 2018. PMID: 30352934 Free PMC article.
-
Genome-scale analysis of regulatory protein acetylation enzymes from photosynthetic eukaryotes.BMC Genomics. 2017 Jul 5;18(1):514. doi: 10.1186/s12864-017-3894-0. BMC Genomics. 2017. PMID: 28679357 Free PMC article.
-
The Biological Significance of Targeting Acetylation-Mediated Gene Regulation for Designing New Mechanistic Tools and Potential Therapeutics.Biomolecules. 2021 Mar 18;11(3):455. doi: 10.3390/biom11030455. Biomolecules. 2021. PMID: 33803759 Free PMC article. Review.
-
Protein acetylation and deacetylation in plant-pathogen interactions.Environ Microbiol. 2021 Sep;23(9):4841-4855. doi: 10.1111/1462-2920.15725. Epub 2021 Aug 30. Environ Microbiol. 2021. PMID: 34398483 Review.
-
mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. doi: 10.1073/pnas.1218515110. Epub 2013 Apr 9. Proc Natl Acad Sci U S A. 2013. PMID: 23572591 Free PMC article.
Cited by
-
Protein Acetylation at the Interface of Genetics, Epigenetics and Environment in Cancer.Metabolites. 2021 Apr 1;11(4):216. doi: 10.3390/metabo11040216. Metabolites. 2021. PMID: 33916219 Free PMC article. Review.
-
Tailoring a CRISPR/Cas-based Epigenome Editor for Programmable Chromatin Acylation and Decreased Cytotoxicity.bioRxiv [Preprint]. 2024 Sep 22:2024.09.22.611000. doi: 10.1101/2024.09.22.611000. bioRxiv. 2024. PMID: 39345554 Free PMC article. Preprint.
-
The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7.Nucleic Acids Res. 2022 Mar 21;50(5):2587-2602. doi: 10.1093/nar/gkac083. Nucleic Acids Res. 2022. PMID: 35137201 Free PMC article.
-
Emerging Role of Epigenetic Modifiers in Breast Cancer Pathogenesis and Therapeutic Response.Cancers (Basel). 2023 Aug 7;15(15):4005. doi: 10.3390/cancers15154005. Cancers (Basel). 2023. PMID: 37568822 Free PMC article. Review.
-
KAT3-dependent acetylation of cell type-specific genes maintains neuronal identity in the adult mouse brain.Nat Commun. 2020 May 22;11(1):2588. doi: 10.1038/s41467-020-16246-0. Nat Commun. 2020. PMID: 32444594 Free PMC article.
References
-
- Kleff, S., Andrulis, E. D., Anderson, C. W. & Sternglanz, R. Identification of a gene encoding a yeast histone H4 acetyltransferase. J. Biol. Chem. 270, 24674–24677 (1995). - PubMed
-
- Brownell, J. E. et al. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84, 843–851 (1996). - PubMed
-
- Kuo, M. H. et al. Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines. Nature 383, 269–272 (1996). - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous