Assembly of major histocompatibility complex class II subunits with invariant chain.

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 Lett

journal_title

FEBS letters

authors

Neumann J,Koch N

doi

10.1016/j.febslet.2005.09.070

keywords:

subject

Has Abstract

pub_date

2005-11-07 00:00:00

pages

6055-9

issue

27

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(05)01188-9

journal_volume

579

pub_type

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