Ubiquitination of gasdermin D N-terminal domain directs its membrane translocation and pore formation during pyroptosis

Abstract excerpt

<title>Abstract</title> <p>Gasdermin D (GSDMD) is a critical mediator of pyroptosis, which consists of a N-terminal pore-forming domain and a C-terminal autoinhibitory domain. The free N-terminal domain (GD-NT), which is released through caspase-1/11 cleavage, exhibits distinct features from the full-length GSDMD (GD-FL), including oligomerization, membrane translocation and pore-formation. However, the underlyin...

Topics

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• Apoptosis Regulatory Proteins
• Crystallography, X-Ray
• Inflammasome and immune disorders
• Intracellular Signaling Peptides and Proteins
• Models, Molecular
• Neoplasm Proteins
• Phosphate-Binding Proteins
• Protein Domains

Identifiers and source

Literature Corpus work

890091f8-a09b-5e0c-8983-388a884187d3

DOI

10.21203/rs.3.rs-4907061/v1