Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person MHC II alpha beta dimers associate with a third polypeptide,...
| Class:Id | Summation:2130631 |
|---|---|
| _displayName | MHC II alpha beta dimers associate with a third polypeptide,... |
| _timestamp | 2012-05-03 15:22:52 |
| created | [InstanceEdit:2130630] Garapati, P V, 2012-02-21 |
| literatureReference | [LiteratureReference:2130535] Interaction of MHC class II molecules with the invariant chain: role of the invariant chain (81-90) region [LiteratureReference:2130329] MHC II and the endocytic pathway: regulation by invariant chain [LiteratureReference:2130674] The segment of invariant chain that is critical for association with major histocompatibility complex class II molecules contains the sequence of a peptide eluted from class II polypeptides [LiteratureReference:2130510] Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding [LiteratureReference:2130319] A role for calnexin (IP90) in the assembly of class II MHC molecules [LiteratureReference:2130526] Class II histocompatibility molecules associate with calnexin during assembly in the endoplasmic reticulum [LiteratureReference:2213064] Sequence analysis of peptides bound to MHC class II molecules [LiteratureReference:2132037] How MHC class II molecules acquire peptide cargo: biosynthesis and trafficking through the endocytic pathway [LiteratureReference:2220953] Mapping functional regions in the lumenal domain of the class II-associated invariant chain |
| modified | [InstanceEdit:2213059] Garapati, P V, 2012-04-30 [InstanceEdit:2220950] Jupe, S, 2012-05-03 [InstanceEdit:2220954] Garapati, P V, 2012-05-03 |
| text | MHC II alpha beta dimers associate with a third polypeptide, the invariant chain (Ii), required for class II molecules to reach the endocytic pathway (Roche et al. 1991). The interaction of Ii with the MHC II alpha beta dimer serves multiple functions. It plays a role in assembly, folding, egress from the ER and transport through the Golgi. Ii exists as a trimer; residues 163-183 of the Ii lumenal domain are involved in covalent cross-linking. Residues 96-104 are critical for association with class II alpha beta dimers (Bijlmakers et al. 1994, Freisewinkel et al. 1993). Residues 89-104 known as CLIP (Class II-associated invariant chain peptide) are the part of the Ii chain that binds antigen binding MHC class II groove, remaining bound until the MHC receptor is completely assembled. This CLIP domain prevents the premature binding of self-peptide fragments present in ER prior to MHC II localization within the endosomal compartment. The ER-resident chaperone protein calnexin rapidly associates with newly synthesized alpha, beta and invariant chains, and remains associated until the final nonamer assembly. The stoichiometry of calnexin in this interaction and the dynamics of association-dissociation are not known. Calnexin may stabilize the free class II chains and regulate their intracellular transport by facilitating the production of transport competent molecules out of the ER (Anderson & Cresswell 1994, Schreiber et al. 1995). |
| (summation) | [Reaction:2130478] Interaction of invariant chain trimer and MHC II alpha beta dimer [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by MHC II alpha beta dimers associate with a third polypeptide,... (2130631)
