- 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...
Expand abstract - Publisher copy:
- 10.1016/j.molcel.2014.03.018
-
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- Publisher:
- Cell Press
- Journal:
- Molecular Cell
- Volume:
- 54
- Issue:
- 3
- Pages:
- 335-348
- Publication date:
- 2014-05-08
- DOI:
- EISSN:
-
1097-4164
- ISSN:
-
1097-2765
- URN:
-
uuid:084c4f45-3ca1-4aa8-856c-6da53c26ab4f
- Source identifiers:
-
467173
- Local pid:
- pubs:467173
- Language:
- English
- Copyright date:
- 2014
Journal article
Molecular basis and regulation of OTULIN-LUBAC interaction
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