NLRP11 attenuates Toll-like receptor signalling by targeting TRAF6 for degradation via the ubiquitin ligase RNF19A

Chenglei Wu, Zexiong Su, Meng Lin, Jiayu Ou, Wei Zhao, Jun Cui () and Rong-Fu Wang ()
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Chenglei Wu: Sun Yat-sen University
Zexiong Su: State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University
Meng Lin: State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University
Jiayu Ou: Sun Yat-sen University
Wei Zhao: Sun Yat-sen University
Jun Cui: State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University
Rong-Fu Wang: Houston Methodist Research Institute

Nature Communications, 2017, vol. 8, issue 1, 1-15

Abstract: Abstract The adaptor protein TRAF6 has a central function in Toll-like receptor (TLR) signalling, yet the molecular mechanisms controlling its activity and stability are unclear. Here we show that NLRP11, a primate specific gene, inhibits TLR signalling by targeting TRAF6 for degradation. NLRP11 recruits the ubiquitin ligase RNF19A to catalyze K48-linked ubiquitination of TRAF6 at multiple sites, thereby leading to the degradation of TRAF6. Furthermore, deficiency in either NLRP11 or RNF19A abrogates K48-linked ubiquitination and degradation of TRAF6, which promotes activation of NF-κB and MAPK signalling and increases the production of proinflammatory cytokines. Therefore, our findings identify NLRP11 as a conserved negative regulator of TLR signalling in primate cells and reveal a mechanism by which the NLRP11-RNF19A axis targets TRAF6 for degradation.

Date: 2017
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DOI: 10.1038/s41467-017-02073-3

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