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Details on Person The N‑terminal fragment of gasdermin E (GSDME(1-270)) produc...

Class:Id	Summation:9710258
_displayName	The N‑terminal fragment of gasdermin E (GSDME(1-270)) produc...
_timestamp	2021-01-07 20:02:30
created	[InstanceEdit:9710266] Shamovsky, Veronica, 2020-12-25
literatureReference	[LiteratureReference:9686078] Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death [LiteratureReference:9689630] Gasdermin pores permeabilize mitochondria to augment caspase-3 activation during apoptosis and inflammasome activation [LiteratureReference:9686122] Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a gasdermin [LiteratureReference:9647685] Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores [LiteratureReference:9647670] Mechanisms of Gasdermin Family Members in Inflammasome Signaling and Cell Death [LiteratureReference:9647674] Pore-forming activity and structural autoinhibition of the gasdermin family [LiteratureReference:9693533] Mechanism of membrane pore formation by human gasdermin-D [LiteratureReference:9647669] Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
modified	[InstanceEdit:9711033] Shamovsky, Veronica, 2021-01-07
text	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).
(summation)	[Reaction:9710254] GSDME oligomerizes [Homo sapiens]
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