Reduction of disulphide bonds in MHC II antigens

Stable Identifier
Reaction [transition]
Homo sapiens
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MHC class II epitopes require protein denaturation and removal of intra- and inter-chain disulphide bonds prior to proteolysis. The lysosomal thiol reductase gamma-IFN-inducible lysosomal thiol reductase (GILT) has been shown to facilitate MHC class II-restricted antigen (Ag) processing by breaking disulphide bonds. GILT is constitutively expressed in APCs. The reduction of disulphide bonds by mature GILT is optimal at acidic pH (Hastings et al. 2006, Arunachalam et al. 2000).

Literature References
PubMed ID Title Journal Year
10639150 Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT)

Arunachalam, B, Phan, UT, Cresswell, P, Geuze, HJ

Proc Natl Acad Sci U S A 2000
17142755 Functional requirements for the lysosomal thiol reductase GILT in MHC class II-restricted antigen processing

Lackman, RL, Cresswell, P, Hastings, KT

J Immunol 2006
Catalyst Activity

oxidoreductase activity, acting on a sulfur group of donors of IFI30 [lysosomal lumen]

Orthologous Events
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