Ontology highlight
ABSTRACT:
SUBMITTER: Karmakar M
PROVIDER: S-EPMC7200749 | biostudies-literature | 2020 May
REPOSITORIES: biostudies-literature
Karmakar Mausita M Minns Martin M Greenberg Elyse N EN Diaz-Aponte Jose J Pestonjamasp Kersi K Johnson Jennifer L JL Rathkey Joseph K JK Abbott Derek W DW Wang Kun K Shao Feng F Catz Sergio D SD Dubyak George R GR Pearlman Eric E
Nature communications 20200505 1
Gasdermin-D (GSDMD) in inflammasome-activated macrophages is cleaved by caspase-1 to generate N-GSDMD fragments. N-GSDMD then oligomerizes in the plasma membrane (PM) to form pores that increase membrane permeability, leading to pyroptosis and IL-1β release. In contrast, we report that although N-GSDMD is required for IL-1β secretion in NLRP3-activated human and murine neutrophils, N-GSDMD does not localize to the PM or increase PM permeability or pyroptosis. Instead, biochemical and microscopy ...[more]