Reactome | GSDMD (1-275) binds bacterial cardiolipin

GSDMD (1-275) binds bacterial cardiolipin

Stable Identifier

R-HSA-9647643

Type

Reaction [binding]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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GSDMD (1-275) binds bacterial cardiolipin

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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.

Literature References

PubMed ID	Title	Journal	Year
27281216	Pore-forming activity and structural autoinhibition of the gasdermin family Wang, DC, Ding, J, Liu, W, Shi, J, Shao, F, Wang, K, Sun, Q, Sun, H, She, Y	Nature	2016
27383986	Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores Lieberman, J, Wu, H, Zhang, Z, Magupalli, VG, Ruan, J, Pan, Y, Liu, X	Nature	2016