Abstract:
:The highly polymorphic major histocompatibility complex class II (MHCII) polypeptides assemble in the ER with the assistance of invariant chain (Ii) chaperone. Ii binds to the peptide-binding pocket of MHCII heterodimers. We explored the mechanism how MHCII subunits attach to Ii. Expression with single alpha or beta subunits from three human HLA and two mouse H2 class II isotypes revealed that Ii co-isolates predominantly with the alpha polypeptide. Co-isolation with alpha chain requires the groove binding Ii-segment and depends on M91 of Ii. Immunoprecipitation of Ii from pulse chase labeled cells showed sequential assembly of alpha and beta chains.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Neumann J,Koch Ndoi
10.1016/j.febslet.2005.09.070keywords:
subject
Has Abstractpub_date
2005-11-07 00:00:00pages
6055-9issue
27eissn
0014-5793issn
1873-3468pii
S0014-5793(05)01188-9journal_volume
579pub_type
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