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Gasdermin D is a member of the gasdermin family.
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These findings reveal that GSDMD-C acts as an auto-inhibition executor and GSDMD-N could form pore structures via a charge-charge interaction upon cleavage by caspases during cell pyroptosis.
This study reveals the pore-forming activity of GSDMD and channel-forming activity of MLKL determine different ways of plasma membrane rupture in pyroptosis and necroptosis.
GsdmD p30 kills cells by forming pores that compromise the integrity of the cell membrane.
Data, including data from studies using recombinant fusion forms of GSDMD, suggest that GSDMD participates in inflammasome-dependent pyroptosis of macrophages in response to various stimuli; this mechanism involves proteolysis of GSDMD by caspase-1 (显示 CASP1 ELISA试剂盒) and caspase-11 (显示 CASP4 ELISA试剂盒).
Remarkably, the Enterovirus 71 protease 3C directly targets GSDMD and induces its cleavage, which is dependent on the protease activity.
The pyroptosis is redefined as gasdermin D-mediated programmed necrosis. Gasdermin D are associated with various genetic diseases, and their cellular function and mechanism of activation.
Overall, these data demonstrate that GSDMD is the direct and final executor of pyroptotic cell death.
Studies show that the membrane-pores composed of gasdermin D-N domains (GSDMD-N domain) are required for pyroptosis.
Studies indicate that gasdermin D (GSDMD) is cleaved by the activated caspases-1/4/5/11 between its N-terminal and C-terminal domains.
Gene deletion of GSDMD demonstrated that GSDMD is required for pyroptosis and for the secretion but not proteolytic maturation of IL-1beta (显示 IL1B ELISA试剂盒) in both canonical and non-canonical inflammasome responses.
identification of gasdermin D (Gsdmd) by genome-wide clustered regularly interspaced palindromic repeat (CRISPR)-Cas9 nuclease screens of caspase-11 (显示 CASP4 ELISA试剂盒)- and caspase-1 (显示 CASP1 ELISA试剂盒)-mediated pyroptosis in mouse bone marrow macrophages
gasdermin D is essential for caspase-11-dependent pyroptosis and interleukin-1beta maturation
This study clearly shows that Gsdmd is not essential for development of mouse intestinal tract or epithelial cell differentiation.
Gasdermin D is a member of the gasdermin family. Members of this family appear to play a role in regulation of epithelial proliferation. Gasdermin D has been suggested to act as a tumor suppressor. Alternatively spliced transcript variants have been described.
gasdermin domain containing 1
, gasdermin D
, gasdermin domain-containing protein 1