DPP9's Enzymatic Activity and Not Its Binding to CARD8 Inhibits Inflammasome Activation.

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ID: 51448
2019
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Abstract
Inflammasomes are multiprotein complexes formed in response to pathogens. NLRP1 and CARD8 are related proteins that form inflammasomes, but the pathogen-associated signal(s) and the molecular mechanisms controlling their activation have not been established. Inhibitors of the serine dipeptidyl peptidases DPP8 and DPP9 (DPP8/9) activate both NLRP1 and CARD8. Interestingly, DPP9 binds directly to NLRP1 and CARD8, and this interaction may contribute to the inhibition of NLRP1. Here, we use activity-based probes, reconstituted inflammasome assays, and mass spectrometry-based proteomics to further investigate the DPP9-CARD8 interaction. We show that the DPP9-CARD8 interaction, unlike the DPP9-NLRP1 interaction, is not disrupted by DPP9 inhibitors or CARD8 mutations that block autoproteolysis. Moreover, wild-type, but not catalytically inactive mutant, DPP9 rescues CARD8-mediated cell death in knockout cells. Together, this work reveals that DPP9's catalytic activity and not its binding to CARD8 restrains the CARD8 inflammasome and thus suggests the binding interaction likely serves some other biological purpose.
Reference Key
griswold2019dpp9sacs Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Griswold, Andrew R;Ball, Daniel P;Bhattacharjee, Abir;Chui, Ashley J;Rao, Sahana D;Taabazuing, Cornelius Y;Bachovchin, Daniel A;
Journal ACS chemical biology
Year 2019
DOI
10.1021/acschembio.9b00462
URL
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