Gsdmc
Domain
Intramolecular interactions between N- and C-terminal domains are important for autoinhibition in the absence of activation signal. The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain.
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.
Post-translational modifications
Cleavage by CASP8 relieves autoinhibition by releasing the N-terminal moiety (Gasdermin-C, N-terminal) that initiates pyroptosis.
Palmitoylated.
Sequence Similarities
Belongs to the gasdermin family.
Cellular localization
- Gasdermin-C
- Cytoplasm
- Cytosol
- Gasdermin-C, N-terminal
- Cell membrane
- Multi-pass membrane protein
Alternative names
Gsdmc1, Mlze, Gsdmc, Gasdermin-C, Gasdermin-C1, Melanoma-derived leucine zipper-containing extranuclear factor, mMLZE