Reactome | The N-terminal domain of gasdermin D (GSDMD(1-275), also kno...

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created	[InstanceEdit:9647682] Shamovsky, Veronica, 2019-06-03
dbId	9647673
displayName	The N-terminal domain of gasdermin D (GSDMD(1-275), also kno...
literatureReference	[LiteratureReference:9647685] Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores [LiteratureReference:9647674] Pore-forming activity and structural autoinhibition of the gasdermin family [LiteratureReference:9689630] Gasdermin pores permeabilize mitochondria to augment caspase-3 activation during apoptosis and inflammasome activation
modified	[InstanceEdit:9728823] Shamovsky, Veronica, 2021-04-22
schemaClass	Summation
text	The N-terminal domain of gasdermin D (GSDMD(1-275), also known as GSDMD-NT) binds to cardiolipin, a lipid found on the bacterial cell membrane, and oligomerizes to form pores on the bacterial cell membrane (Ding J et al. 2016; Liu X et al. 2016). GSDMD(1-275) was reported to damage and lyse Gram-positive and Gram-negative bacteria directly, including Escherichia coli, Staphylococcus aureus and Bacillus megaterium protoplasts (Ding J et al. 2016; Liu X et al. 2016). GSDMD(1-275) also interacts with cardiolipin present in the inner leaflet of the host mitochondrial membrane (Rogers C et al. 2019). However, it is not known how GSDMD can pass the outer membrane to access the inner member if it can disrupt the bacterial and mitochondrial membrane under physiological conditions.

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