Ubiquitin code assembly and disassembly.

Claire Heride, Sylvie Urbé, Michael J Clague

Journal: Current biology : CB 2014;24(6):R215-20

PMID: 24650902

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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.

Address: Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, L69 3BX, UK.; Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, L69 3BX, UK. Electronic address: [email protected].

DOI: 10.1016/j.cub.2014.02.002

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MeSH Terms: Genes, Essential, Genetic Code, HEK293 Cells, Humans, Proteasome Endopeptidase Complex, Saccharomyces cerevisiae, Ubiquitin, Ubiquitin-Specific Proteases, Ubiquitination