Acetylation: a regulatory modification to rival phosphorylation?

doi:10.1093/emboj/19.6.1176

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Acetylation: a regulatory modification to rival phosphorylation?

Tony Kouzarides

Wellcome/CRC Institute and Department of Pathology, Cambridge University, Tennis Court Road, Cambridge CB2 1QR, UK
e-mail: tk106{at}mole.bio.cam.ac.uk

The fact that histones are modified by acetylation has been known for almost 30 years. The recent identification of enzymesthat regulate histone acetylation has revealed a broader use ofthis modification than was suspected previously. Acetylases arenow known to modify a variety of proteins, including transcriptionfactors, nuclear import factors and $alpha$ -tubulin. Acetylation regulatesmany diverse functions, including DNA recognition, protein-proteininteraction and protein stability. There is even a conserved structure,the bromodomain, that recognizes acetylated residues and may serveas 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? Thisreview sets out what we know about the broader substrate specificityand regulation of acetyl- ases and goes on to compare acetylationwith the process of phosphorylation.