title: Specificity and disease in the ubiquitin system.
abstract: Post-translational modification (PTM) of proteins by ubiquitination is an essential cellular regulatory process. Such regulation drives the cell cycle and cell division, signalling and secretory pathways, DNA replication and repair processes and protein quality control and degradation pathways. A huge range of ubiquitin signals can be generated depending on the specificity and catalytic activity of the enzymes required for attachment of ubiquitin to a given target. As a consequence of its importance to eukaryotic life, dysfunction in the ubiquitin system leads to many disease states, including cancers and neurodegeneration. This review takes a retrospective look at our progress in understanding the molecular mechanisms that govern the specificity of ubiquitin conjugation.
authors: MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, DD1 5EH, U.K.
authors: Viduth K
authors: VK
authors: Chaugule
authors: MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, DD1 5EH, U.K. h.walden@dundee.ac.uk.
authors: Helen
authors: H
authors: Walden
mesh_terms: D000818:Animals; D004194:Disease; D005199:Fanconi Anemia / Q000201:enzymology / Q000235:genetics; D006801:Humans; D010300:Parkinson Disease / Q000201:enzymology / Q000235:genetics; D013379:Substrate Specificity; D025801:Ubiquitin / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000235:genetics / Q000378:metabolism
chemical_list: D025801:Ubiquitin; D044767:Ubiquitin-Protein Ligases
keywords: E3 ligase; Fanconi anemia; Parkin; RBR; RING; ubiquitin