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Bulek, Katarzyna; Zhao, Junjie; Liao, Yun; Rana, Nitish; Corridoni, Daniele; Antanaviciute, Agne; Chen, Xing; Wang, Han; Qian, Wen; Miller-Little, William A; Swaidani, Shadi; Tang, Fangqiang; Willard, Belinda B; McCrae, Keith; Kang, Zizhen; Dubyak, George R; Cominelli, Fabio; Simmons, Alison; Pizarro, Theresa T; Li, Xiaoxia
The Journal of clinical investigation, 08/2020, Letnik: 130, Številka: 8Journal Article
Gasdermin D (GSDMD) induces pyroptosis via the pore-forming activity of its N-terminal domain, cleaved by activated caspases associated with the release of IL-1β. Here, we report a nonpyroptotic role of full-length GSDMD in guiding the release of IL-1β-containing small extracellular vesicles (sEVs) from intestinal epithelial cells (IECs). In response to caspase-8 inflammasome activation, GSDMD, chaperoned by Cdc37/Hsp90, recruits the E3 ligase, NEDD4, to catalyze polyubiquitination of pro-IL-1β, serving as a signal for cargo loading into secretory vesicles. GSDMD and IL-1β colocalize with the exosome markers CD63 and ALIX intracellularly, and GSDMD and NEDD4 are required for release of CD63+ sEVs containing IL-1β, GSDMD, NEDD4, and caspase-8. Importantly, increased expression of epithelial-derived GSDMD is observed both in patients with inflammatory bowel disease (IBD) and those with experimental colitis. While GSDMD-dependent release of IL-1β-containing sEVs is detected in cultured colonic explants from colitic mice, GSDMD deficiency substantially attenuates disease severity, implicating GSDMD-mediated release of IL-1β sEVs in the pathogenesis of intestinal inflammation, such as that observed in IBD.
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in: SICRIS
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