| Post Translational Modifications | Cleavage by CASP8 relieves autoinhibition by releasing the N-terminal moiety (Gasdermin-C, N-terminal) that initiates pyroptosis. The cleavage site is unclear. According to a publication, it takes place after Asp-240 in response to alpha-ketoglutarate. Another paper reports cleavage by CASP8 after Asp-365. Palmitoylated. |
| Function | Gasdermin-C: This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-C, N-terminal) binds to membranes and forms pores, triggering pyroptosis. Gasdermin-C, N-terminal: Pore-forming protein that causes membrane permeabilization and pyroptosis. Produced by the cleavage of gasdermin-C by caspase CASP8 in response to death signals. After cleavage, moves to the plasma membrane where it strongly binds to membrane inner leaflet lipids. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis. |
| Protein Name | Gasdermin-CMelanoma-Derived Leucine Zipper-Containing Extranuclear Factor Cleaved Into - Gasdermin-C - N-TerminalGsdmc-Nt - Gasdermin-C - C-TerminalGsdmc-Ct |
| Cellular Localisation | Gasdermin-C: CytoplasmCytosolGasdermin-CN-Terminal: Cell MembraneMulti-Pass Membrane Protein |
| Alternative Protein Names | Gasdermin-C proteinMelanoma-Derived Leucine Zipper-Containing Extranuclear Factor Cleaved Into - Gasdermin-C - N-Terminal proteinGsdmc-Nt - Gasdermin-C - C-Terminal proteinGsdmc-Ct proteinGSDMC proteinMLZE protein |
Information sourced from Uniprot.org
