Oxidized thioredoxin 1 places a leash on NLRP1 inflammasome activity

Immunol Cell Biol. 2024 Jan;102(1):5-7. doi: 10.1111/imcb.12710. Epub 2023 Nov 10.

Abstract

The 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.

Keywords: NACHT domain; TRX1-bound NLRP1 inflammasome; signaling; structure.

MeSH terms

  • Adaptor Proteins, Signal Transducing* / metabolism
  • Apoptosis Regulatory Proteins / metabolism
  • Inflammasomes* / metabolism
  • NLR Proteins
  • Signal Transduction

Substances

  • Inflammasomes
  • Adaptor Proteins, Signal Transducing
  • Apoptosis Regulatory Proteins
  • NLR Proteins