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Selective binding of AIRAPL tandem UIMs to lys48-linked tri-ubiquitin chains

Abstract:

Lys48-linked ubiquitin chains act as the main targeting signals for protein degradation by the proteasome. Here we report selective binding of AIRAPL, a protein that associates with the proteasome upon exposure to arsenite, to Lys48-linked tri-ubiquitin chains. AIRAPL comprises two ubiquitin-interacting motifs in tandem (tUIMs) that are linked through a flexible inter-UIM region. In the complex crystal structure UIM1 binds the proximal ubiquitin, whereas UIM2 (the double-sided UIM) binds n...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/j.str.2015.12.017

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Jenner Institute
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Target Discovery Institute
Role:
Author
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Name:
National Institutes of Health
Grant:
P41GM103393
More from this funder
Name:
US Department of Energy Office of Biological and Environmental Research
Publisher:
Cell Press
Journal:
Structure More from this journal
Volume:
24
Issue:
3
Pages:
412-422
Publication date:
2016-03-01
Acceptance date:
2015-12-20
DOI:
ISSN:
1878-4186
Pubs id:
pubs:604475
UUID:
uuid:6d951a68-dde7-4080-9af3-5c116e5d3d4b
Local pid:
pubs:604475
Source identifiers:
604475
Deposit date:
2016-02-24

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