Reactome | Cleavage of lip22 to lip10

Cleavage of lip22 to lip10

Stable Identifier

R-HSA-2130504

Type

Reaction [transition]

Species

Homo sapiens

Compartment

lysosomal lumen, lysosomal membrane

ReviewStatus

5/5

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The cleavage of lip22 occurs in residues 115-125, closer to the C-terminus than CLIP (residues 81-105). The resulting lip10 fragment is approximately 100 residues long and extends just through the C-terminus of the Ii CLIP. The proteases responsible for generating lip10 in vivo are not determined. Cysteine proteases like cathepsin S (CatS) are capable of degrading lip22 to lip10 (Bania et al. 2003) but in the presence of LHVS, an inhibitor of CatS, lip22 degradation is still observed, suggesting that other proteases are involved (Villadangos et al. 1997), possibly aspartic proteinases such as cathepsins D and E (Kageyama et al. 1996). The degradation of lip22 may depend on cell type (Bania et al. 2003). The lip22 and lip10 intermediate forms are still maintained as a nonameric complex due to the existence of the last trimerisation domain in the transmembrane region.

Literature References

PubMed ID	Title	Journal	Year
12078484	Proteolysis and antigen presentation by MHC class II molecules Bryant, PW, Lennon-Duménil, AM, Fiebiger, E, Lagaudrière-Gesbert, C, Ploegh, HL	Adv Immunol	2002
8687433	Potential sites for processing of the human invariant chain by cathepsins D and E Kageyama, T, Yonezawa, S, Ichinose, M, Miki, K, Moriyama, A	Biochem Biophys Res Commun	1996
11684289	Presentation of antigens by MHC class II molecules: getting the most out of them Villadangos, JA	Mol Immunol	2001
12748383	Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs Bania, J, Gatti, E, Lelouard, H, David, A, Cappello, F, Weber, E, Camosseto, V, Pierre, P	Proc Natl Acad Sci U S A	2003