GSDME oligomerizes

Stable Identifier
Reaction [binding]
Homo sapiens
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The N‑terminal fragment of gasdermin E (GSDME(1-270)) produced by cleavage by caspase-3 (CASP3) or granzyme B (GZMB) targets the plasma membrane (Rogers C et al. 2017; Wang Y et al. 2017). In vitro oligomerization assays showed that GSDME(1-270) formed dimers and high‑molecular weight oligomers when incubated with purified cell membranes from human embryonic kidney 293 (HEK293T) cells (Rogers C et al. 2019). Structural and biochemical studies suggest that the N‑terminal fragments of gasdermins form membrane‑spanning pores allowing release of inflammatory molecules such as interleukin (IL)‑1β, IL‑18, and high‑mobility group box 1 (HMGB1) and eventually causing cell rupture (Shi J et al. 2015; Ding J et al. 2016; Liu X et al. 2016; Feng S et al. 2018; Mulvihill E et al. 2018). Phosphorylation of GSDME at T6 may influence its pore‑forming activity (Rogers C et al. 2019).

Literature References
PubMed ID Title Journal Year
30976076 Gasdermin pores permeabilize mitochondria to augment caspase-3 activation during apoptosis and inflammasome activation

Nardone, A, Aplin, AE, Rogers, C, Erkes, DA, Alnemri, ES, Fernandes-Alnemri, T

Nat Commun 2019
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
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