GSDMD oligomerizes into arc-, slit-shaped structures

Stable Identifier
Reaction [binding]
Homo sapiens
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Gasdermin D (GSDMD) is a member of the gasdermin (GSDM) protein family, which is processed by inflammatory caspases and cleaved into an N‐terminal (GSDMD(1-275)) and a C‐terminal (GSDMD (276-484)) fragments (Shi J et al, 2015). Once GSDMD is cleaved, the N-terminal fragment of GSDMD (1-275) targets and permeabilizes cellular membranes by assembling transmembrane pores (Ding J et al, 2016; Liu X et al, 2016; Sborgi L et al, 2016). High‐resolution (≤ 2 nm) atomic force microscopy (AFM) showed that GSDMD N-terminus inserts into various lipid membranes (Mulvihill E et al. 2018). Once inserted, the N-terminal fragment of GSDMD assembles arc‐, slit‐, and ring‐shaped oligomers, which eventually incorporate additional oligomers and transform into larger thermodynamically stable ring‐shaped oligomers (Mulvihill E et al. 2018).

Literature References
PubMed ID Title Journal Year
29898893 Mechanism of membrane pore formation by human gasdermin-D

Pfreundschuh, M, Mari, SA, Sborgi, L, Hiller, S, Müller, DJ, Mulvihill, E

EMBO J. 2018
This event is regulated
Orthologous Events
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