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YOD1/TRAF6 association balances p62-dependent IL-1 signaling to NF-κB.
eLife 6:e22416 (2017)
The ubiquitin ligase TRAF6 is a key regulator of canonical IκB kinase (IKK)/NF-κB signaling in response to interleukin-1 (IL-1) stimulation. Here, we identified the deubiquitinating enzyme YOD1 (OTUD2) as a novel interactor of TRAF6 in human cells. YOD1 binds to the C-terminal TRAF homology domain of TRAF6 that also serves as the interaction surface for the adaptor p62/Sequestosome-1, which is required for IL-1 signaling to NF-κB. We show that YOD1 competes with p62 for TRAF6 association and abolishes the sequestration of TRAF6 to cytosolic p62 aggregates by a non-catalytic mechanism. YOD1 associates with TRAF6 in unstimulated cells but is released upon IL-1β stimulation, thereby facilitating TRAF6 auto-ubiquitination as well as NEMO/IKKγ substrate ubiquitination. Further, IL-1 triggered IKK/NF-κB signaling and induction of target genes is decreased by YOD1 overexpression and augmented after YOD1 depletion. Hence, our data define that YOD1 antagonizes TRAF6/p62-dependent IL-1 signaling to NF-κB.
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Times Cited
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Nf-kappab ; Cell Biology ; Human ; Interleukin-1 ; Signal Transduction ; Ubiquitin; Ubiquitin-dependent Kinase; Interacting Protein P62; T-cell-activation; Deubiquitinating Enzyme; Polyubiquitin Chain; Sequestosome 1/p62; Ikk Activation; Traf6; Complex; Interleukin-1
Language
english
Publication Year
2017
HGF-reported in Year
2017
ISSN (print) / ISBN
2050-084X
e-ISSN
2050-084X
Journal
eLife
Quellenangaben
Volume: 6,
Article Number: e22416
Publisher
eLife Sciences Publications
Publishing Place
Cambridge
Reviewing status
Peer reviewed
Institute(s)
Research Unit Signaling and Translation (SAT)
Institute of Molecular Toxicology and Pharmacology (TOX)
Institute of Molecular Toxicology and Pharmacology (TOX)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Enabling and Novel Technologies
PSP Element(s)
G-509800-002
G-505293-001
G-505293-001
PubMed ID
28244869
WOS ID
WOS:000396109000001
Scopus ID
85014923360
Erfassungsdatum
2017-04-20