title: Molecular Basis for Histone Acetyltransferase Regulation by Binding Partners, Associated Domains, and Autoacetylation.
abstract: Acetylation is a post-translational modification (PTM) that regulates chromatin dynamics and function. Dysregulation of acetylation or acetyltransferase activity has been correlated with several human diseases. Many, if not all, histone acetyltransferases (HATs) are regulated in part through tethered domains, association with binding partners, or post-translational modification, including predominantly acetylation. This review focuses on what is currently understood at the molecular level of HAT regulation as it occurs via binding partners, associated domains, and autoacetylation.
authors.affiliation: Department of Chemistry, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
authors.forename: Cheryl E
authors.initials: CE
authors.lastname: McCullough
authors.affiliation: Department of Chemistry, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.|Department of Biochemistry & Biophysics, Abramson Family Cancer Research Institute, Perelman School of Medicine at the University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
authors.forename: Ronen
authors.initials: R
authors.lastname: Marmorstein
mesh_terms: D000107:Acetylation; D044127:Epigenesis, Genetic; D015971:Gene Expression Regulation, Enzymologic / Q000502:physiology*; D051548:Histone Acetyltransferases / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D000072417:Protein Domains
chemical_list: D051548:Histone Acetyltransferases