title: Acetylation: a regulatory modification to rival phosphorylation?
abstract: The fact that histones are modified by acetylation has been known for almost 30 years. The recent identification of enzymes that regulate histone acetylation has revealed a broader use of this modification than was suspected previously. Acetylases are now known to modify a variety of proteins, including transcription factors, nuclear import factors and alpha-tubulin. Acetylation regulates many diverse functions, including DNA recognition, protein-protein interaction and protein stability. There is even a conserved structure, the bromodomain, that recognizes acetylated residues and may serve as a signalling domain. If you think all this sounds familiar, it should be. These are features characteristic of kinases. So, is acetylation a modification analogous to phosphorylation? This review sets out what we know about the broader substrate specificity and regulation of acetyl- ases and goes on to compare acetylation with the process of phosphorylation.
authors.affiliation: Wellcome/CRC Institute, Department of Pathology, Cambridge University, Tennis Court Road, Cambridge CB2 1QR, UK. tk106@mole.bio.cam.ac.uk
authors.forename: T
authors.initials: T
authors.lastname: Kouzarides
mesh_terms: D000107:Acetylation; D000115:Acetylesterase / Q000378:metabolism; D000123:Acetyltransferases / Q000378:metabolism; D000581:Amidohydrolases / Q000378:metabolism; D006657:Histones / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D006657:Histones; D011506:Proteins; D000123:Acetyltransferases; D000115:Acetylesterase; D000581:Amidohydrolases