title: Ubiquitin code assembly and disassembly.
abstract: Ubiquitin, a 76 amino-acid polypeptide, presents a compact three-dimensional structure, utilising a fold that recurs within larger polypeptides and in other protein modifiers, such as NEDD8 and SUMO. Ubiquitylation was initially recognised as a signal for proteasome-mediated degradation. We shall consider here how this view has evolved to appreciate that the dynamic appendage of different types of ubiquitin chains represents a versatile, three-dimensional code, fundamental to the control of many cellular processes.
authors.affiliation: Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, L69 3BX, UK.
authors.forename: Claire
authors.initials: C
authors.lastname: Heride
authors.affiliation: Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, L69 3BX, UK.
authors.forename: Sylvie
authors.initials: S
authors.lastname: Urbé
authors.affiliation: Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, L69 3BX, UK. Electronic address: clague@liv.ac.uk.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Clague
mesh_terms: D020043:Genes, Essential; D005815:Genetic Code; D057809:HEK293 Cells; D006801:Humans; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D025801:Ubiquitin / Q000096:biosynthesis* / Q000378:metabolism; D064570:Ubiquitin-Specific Proteases / Q000378:metabolism; D054875:Ubiquitination
chemical_list: D025801:Ubiquitin; D064570:Ubiquitin-Specific Proteases; D046988:Proteasome Endopeptidase Complex