Reactome | Reduction of disulphide bonds in MHC II antigens

Reduction of disulphide bonds in MHC II antigens

Stable Identifier

R-HSA-2213240

Type

Reaction [transition]

Species

Homo sapiens

Compartment

lysosomal lumen

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Reduction of disulphide bonds in MHC II antigens

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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