Abstract
Ubiquitylation is a post-translational modification implicated in several different cellular pathways. The possibility of forming chains through covalent crosslinking between any of the seven lysines, or the initial methionine, and the C terminus of another moiety provides ubiquitin (Ub) with special flexibility in its function in signalling. Here, we review the knowledge accumulated over the past several years about the functions and structural features of polyUb chains. This analysis reveals the need to understand further the functional role of some of the linkages and the structural code that determines recognition of polyUbs by protein partners.
Keywords:
biophysics; post-translational modifications; proteasomal pathway; signalling; structure; ubiquitin.
Crown Copyright © 2016. Published by Elsevier Ltd. All rights reserved.
Publication types
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Review
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Animals
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Binding Sites
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Endopeptidases / chemistry*
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Endopeptidases / genetics
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Endopeptidases / metabolism
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Humans
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Hydrophobic and Hydrophilic Interactions
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Lysine / metabolism
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NEDD8 Protein
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Polyubiquitin / chemistry*
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Polyubiquitin / genetics
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Polyubiquitin / metabolism
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Proteasome Endopeptidase Complex / metabolism
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Protein Binding
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Protein Conformation, alpha-Helical
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Protein Conformation, beta-Strand
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Protein Interaction Domains and Motifs
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Protein Processing, Post-Translational*
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Signal Transduction
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Small Ubiquitin-Related Modifier Proteins / chemistry*
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Small Ubiquitin-Related Modifier Proteins / genetics
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Small Ubiquitin-Related Modifier Proteins / metabolism
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Ubiquitin / chemistry*
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Ubiquitin / genetics
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Ubiquitin / metabolism
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Ubiquitination
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Ubiquitins / chemistry*
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Ubiquitins / genetics
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Ubiquitins / metabolism
Substances
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NEDD8 Protein
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NEDD8 protein, human
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Small Ubiquitin-Related Modifier Proteins
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Ubiquitin
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Ubiquitins
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Polyubiquitin
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Endopeptidases
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Proteasome Endopeptidase Complex
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Lysine