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Growing a gasdermin pore in membranes of pyroptotic cells
Author(s) -
Ding Jingjin,
Shao Feng
Publication year - 2018
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.2018100067
Subject(s) - pyroptosis , beijing , chinese academy of sciences , china , excellence , library science , center of excellence , inflammasome , political science , biology , law , immunology , computer science , inflammation
Inflammasome‐activated caspase‐1, caspase‐11, caspase‐4, and caspase‐5 cleave GSDMD to unleash its N‐terminal gasdermin‐N domain ( GSDMD N term ) that perforates the plasma membrane to execute pyroptosis and stimulate inflammation. The mechanism underlying GSDMD N term pore formation is unclear. Mulvihill et al use high‐resolution atomic force microscopy ( AFM ) to analyze the dynamic pore formation process of GSDMD N term . GSDMD N term protomers are inserted into the lipid membrane to assemble arc‐ or slit‐shaped oligomers that can incorporate additional protomers and grow into large and stable ring‐shaped oligomers to form pores.