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Gasdermin pores permeabilize mitochondria to augment caspase-3 activation during apoptosis and inflammasome activation
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Gasdermin pores permeabilize mitochondria to augment caspase-3 activation during apoptosis and inflammasome activation
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Journal Article
Gasdermin pores permeabilize mitochondria to augment caspase-3 activation during apoptosis and inflammasome activation
2019
Overview
Gasdermin E (GSDME/DFNA5) cleavage by caspase-3 liberates the GSDME-N domain, which mediates pyroptosis by forming pores in the plasma membrane. Here we show that GSDME-N also permeabilizes the mitochondrial membrane, releasing cytochrome c and activating the apoptosome. Cytochrome c release and caspase-3 activation in response to intrinsic and extrinsic apoptotic stimuli are significantly reduced in GSDME-deficient cells comparing with wild type cells. GSDME deficiency also accelerates cell growth in culture and in a mouse model of melanoma. Phosphomimetic mutation of the highly conserved phosphorylatable Thr6 residue of GSDME, inhibits its pore-forming activity, thus uncovering a potential mechanism by which GSDME might be regulated. Like GSDME-N, inflammasome-generated gasdermin D-N (GSDMD-N), can also permeabilize the mitochondria linking inflammasome activation to downstream activation of the apoptosome. Collectively, our results point to a role of gasdermin proteins in targeting the mitochondria to promote cytochrome c release to augment the mitochondrial apoptotic pathway.
Gasdermins mediate lytic cell death by forming pores in the plasma membrane. Here the authors show that gasdermins also permeabilize mitochondrial membrane, thereby facilitating intrinsic apoptosis pathway, downstream of apoptotic (Gasdermin E) and inflammatory (Gasdermin D) caspase activation.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/19
/ 14/35
/ 14/63
/ 82/1
/ 82/29
/ 96/106
/ 96/2
/ 96/95
/ Animals
/ Caspase
/ Humanities and Social Sciences
/ Humans
/ Melanoma
/ Melanoma, Experimental - pathology
/ Mice
/ Mitochondrial Membranes - metabolism
/ Mutation
/ Phosphorylation - physiology
/ Pores
/ Proteins
/ Receptors, Estrogen - genetics
/ Receptors, Estrogen - metabolism
/ Science
