Gasdermin-C2
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-C2
This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-C2, N-terminal) binds to membranes and forms pores, triggering pyroptosis.
Gasdermin-C2, N-terminal
Pore-forming protein that causes membrane permeabilization and pyroptosis in response to type-2 immunity (PubMed:34290141). Produced by the cleavage of gasdermin-C2 in response to type-2 immunity following worm infection (PubMed:34290141). After cleavage, moves to the plasma membrane where it strongly binds to membrane inner leaflet lipids (By similarity). Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis and lytic cell death in enterocytes (PubMed:34290141).
Post-translational modifications
Cleavage by CASP8 relieves autoinhibition by releasing the N-terminal moiety (Gasdermin-C2, N-terminal) that initiates pyroptosis (PubMed:34290141).
Palmitoylated.
Sequence Similarities
Belongs to the gasdermin family.
Cellular localization
- Gasdermin-C2
- Cytoplasm
- Cytosol
- Gasdermin-C2, N-terminal
- Cell membrane
- Multi-pass membrane protein
Alternative names
Gasdermin-C2, Gsdmc2