Oxidized thioredoxin 1 places a leash on NLRP1 inflammasome activity

Author:

Yap Jeremy KY1,Emming Stefan1,Schroder Kate1

Affiliation:

1. Centre for Cell Biology of Chronic Disease, Institute for Molecular Bioscience The University of Queensland St Lucia QLD Australia

Abstract

AbstractThe biology of the NACHT domain and leucine‐rich repeat (NLR) and pyrin domain‐containing 1 (NLRP1) inflammasome has perplexed researchers since this inflammasome was first described about two decades ago. The identification of oxidized thioredoxin 1 (TRX1) as a suppressor of NLRP1 recently linked cellular redox homeostasis to NLRP1 inflammasome signaling. Now, Zhang et al. present a molecular structure of TRX1‐bound NLRP1 with unprecedented detail. This structure gives key insight into regulatory mechanisms governing NLRP1 activation and offers enormous potential for structure‐based anti‐inflammatory drug design.

Publisher

Wiley

Subject

Cell Biology,Immunology,Immunology and Allergy

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