Gasdermin B (GSDMB) is a pore-forming protein that executes pyroptosis, a proinflammatory programmed necrotic cell death, when cleaved by specific proteases. Unlike gasdermin D, GSDMB is activated by inflammasome-independent mechanisms 1. Granzyme A (GZMA) from cytotoxic lymphocytes cleaves GSDMB to trigger pyroptosis in target cells, with interferon-γ upregulating GSDMB expression to promote this killing mechanism 2. GSDMB contains multiple splicing isoforms; those with exon 6 exhibit pore-forming pyroptotic activity, while non-canonical isoforms lack this function 3. The gasdermin-N domain binds membrane lipids and phosphoinositides to form 10-14 nm pores containing 16 symmetric protomers 4. Beyond pyroptosis, GSDMB regulates epithelial restitution and repair in inflammatory bowel disease independent of pyroptotic mechanisms, promoting epithelial cell proliferation and migration through PDGF-A-mediated FAK signaling 5. Disease-associated GSDMB genetic variants impair epithelial barrier function restoration. Genome-wide association studies identified GSDMB genetic markers associated with childhood-onset asthma susceptibility 6. GSDMB participates in pyroptotic pathways implicated in respiratory diseases including asthma, COPD, and acute lung injury 7. Pathogenic bacteria like Shigella flexneri utilize ubiquitin-ligase IpaH7.8 to degrade human GSDMB, highlighting its immunological significance 3.