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Curr Biol. 2014 Mar 17;24(6):R215-20. doi: 10.1016/j.cub.2014.02.002.

Ubiquitin code assembly and disassembly.

Author information

1
Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, L69 3BX, UK.
2
Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, L69 3BX, UK. Electronic address: clague@liv.ac.uk.

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.

PMID:
24650902
DOI:
10.1016/j.cub.2014.02.002
[Indexed for MEDLINE]
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