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Molecular basis and regulation of OTULIN-LUBAC interaction

Abstract:

The linear ubiquitin (Ub) chain assembly complex (LUBAC) generates Met1-linked "linear" Ub chains that regulate the activation of the nuclear factor κB (NFκB) transcription factor and other processes. We recently discovered OTULIN as a deubiquitinase that specifically cleaves Met1-linked polyUb. Now, we show that OTULIN binds via a conserved PUB-interacting motif (PIM) to the PUB domain of the LUBAC component HOIP. Crystal structures and nuclear magnetic resonance experiments reveal the molec...

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Publisher:
Cell Press
Journal:
Molecular Cell More from this journal
Volume:
54
Issue:
3
Pages:
335-348
Publication date:
2014-05-08
DOI:
EISSN:
1097-4164
ISSN:
1097-2765
Language:
English
Pubs id:
pubs:467173
UUID:
uuid:084c4f45-3ca1-4aa8-856c-6da53c26ab4f
Local pid:
pubs:467173
Source identifiers:
467173
Deposit date:
2014-07-20

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