Pore-forming activity and structural autoinhibition of the gasdermin family

By Jingjin Ding, Kun Wang, Wang Liu, Yang She, Qi Sun, Jianjin Shi, Hanzi Sun, Dacheng Wang, F. Shao. Nature, 2016

1,946 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology, Parasitology

View Paper: https://www.semanticscholar.org/paper/b8155752fa6dbf1fd0a524ccbf06c615344fdbb1

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In Immunology

In Molecular Biology

Citations in the corpus

Pyroptosis in inflammatory diseases and cancer (2022, background): “All gasdermins except DFNB59 have two conserved domains, an N-terminal effector domain and a C-terminal inhibitory domain [11].”
Molecular mechanisms of cell death in neurological diseases (2021, background): “Caspase-1 cleaves GSDMD and its Nterminal fragment assembles into a plasma membrane pore [136].”
Target highlights from the first post-PSI CASP experiment (CASP12, May–August 2016) (2017, neutral): “This Gsdma3 region is functionally important because it interacts with a segment on the N-terminal domain that is involved in membrane disruption.(64) A total of 422 predictions for T0948 were deposited in CASP12, and 150 of them had GDT_TS scores>70.”
Pyroptosis: Gasdermin-Mediated Programmed Necrotic Cell Death. (2017, background): “The gasdermin-N domains of GSDMA/GSDMA3, GSDMB, GSDMC, and DFNA5, but not the full-length protein, all can induce mammalian cell pyroptosis and kill bacteria [29,35].”
Caspases in cell death, inflammation and disease (2019, background): “The gasdermin family consists of several members that exert the ability to form large oligomeric membrane pores with an inner diameter of 12-20 nm in the inner layer of the plasma membrane and intracellular organelles (Ding et al., 2016; Mulvihill et al., 2018; Rogers et al., 2017; Sborgi et al., 20”
The pore forming protein gasdermin D regulates interleukin-1 secretion from living macrophages (2017, neutral): “Upon cleavage, the N-terminal fragment of GSDMD oligomerizes into ring-shaped structures in membranes (Aglietti et al., 2016; Ding et al., 2016; Liu et al., 2016; Sborgi et al., 2016).”
Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death (2017, neutral): “6b) 10 , which is 19.7% sequence identical to DFNA5.”
A guide to cell death pathways (2023, neutral): “The pores formed by 16 GSDMD N-domain protomers have an inner diameter of 10–14 nm, which can mediate the release of cytokines without signal peptides such as mature IL-1β in living cells as well as necrosis 109,110 .”
Gasdermins: Effectors of pyroptosis (2017, background): “Gasdermin D does not bind the non-charged head group lipid phosphatidylinositol (PI) or the positively charged head group lipids phosphatidylcholine (PC) and phosphatidylethanolamine (PE)[15,18].”