GSDMD (1-275) binds bacterial cardiolipin

Stable Identifier
Reaction [binding]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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
Orthologous Events
Cite Us!