UBDs [Ub (ubiquitin)-binding domains], which are typically small protein motifs of <50 residues, are used by receptor proteins to transduce post-translational Ub modifications in a wide range of biological processes, including NF-κB (nuclear factor κB) signalling and proteasomal degradation pathways. More than 20 families of UBDs have now been characterized in structural detail and, although many recognize the canonical Ile44/Val70-binding patch on Ub, a smaller number have alternative Ub-recognition sites. The A20 Znf (A20-like zinc finger) of the ZNF216 protein is one of the latter and binds with high affinity to a polar site on Ub centred around Asp58/Gln62. ZNF216 shares some biological function with p62, with both linked to NF-κB signal activation and as shuttle proteins in proteasomal degradation pathways. The UBA domain (Ub-associated domain) of p62, although binding to Ub through the Ile44/Val70 patch, is unique in forming a stable dimer that negatively regulates Ub recognition. We show that the A20 Znf and UBA domain are able to form a ternary complex through independent interactions with a single Ub molecule, supporting functional models for Ub as a ‘hub’ for mediating multi-protein complex assembly and for enhancing signalling specificity.
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April 2012
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Conference Article|
March 21 2012
Structural insights into specificity and diversity in mechanisms of ubiquitin recognition by ubiquitin-binding domains
Mark S. Searle;
Mark S. Searle
1
*Centre for Biomolecular Sciences, School of Chemistry, University of Nottingham, Nottingham NG7 2RD, U.K.
1To whom correspondence should be addressed (emailmark.searle@nottingham.ac.uk).
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Thomas P. Garner;
Thomas P. Garner
*Centre for Biomolecular Sciences, School of Chemistry, University of Nottingham, Nottingham NG7 2RD, U.K.
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Joanna Strachan;
Joanna Strachan
†School of Biomedical Sciences, University of Nottingham Medical School, Nottingham NG7 2UH, U.K.
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Jed Long;
Jed Long
*Centre for Biomolecular Sciences, School of Chemistry, University of Nottingham, Nottingham NG7 2RD, U.K.
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Jennifer Adlington;
Jennifer Adlington
*Centre for Biomolecular Sciences, School of Chemistry, University of Nottingham, Nottingham NG7 2RD, U.K.
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James R. Cavey;
James R. Cavey
†School of Biomedical Sciences, University of Nottingham Medical School, Nottingham NG7 2UH, U.K.
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Barry Shaw;
Barry Shaw
†School of Biomedical Sciences, University of Nottingham Medical School, Nottingham NG7 2UH, U.K.
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Robert Layfield
Robert Layfield
†School of Biomedical Sciences, University of Nottingham Medical School, Nottingham NG7 2UH, U.K.
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Publisher: Portland Press Ltd
Received:
September 06 2011
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem Soc Trans (2012) 40 (2): 404–408.
Article history
Received:
September 06 2011
Citation
Mark S. Searle, Thomas P. Garner, Joanna Strachan, Jed Long, Jennifer Adlington, James R. Cavey, Barry Shaw, Robert Layfield; Structural insights into specificity and diversity in mechanisms of ubiquitin recognition by ubiquitin-binding domains. Biochem Soc Trans 1 April 2012; 40 (2): 404–408. doi: https://doi.org/10.1042/BST20110729
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