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HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH.

Abstract：

:HLA-DM (DM) is a nonclassical MHC class II molecule that interacts with classical MHC II molecules in acidic compartments. During this association DM is supposed to catalyze the release of invariant chain (Ii)-derived CLIP peptides, as well as other peptides bound with low kinetic stability. Here we provide evidence that in lysosomal compartments of B cells a considerable fraction of DM is stably associated with empty DR alphabeta dimers, thereby preventing their functional inactivation and aggregation. Upon encounter with cognate peptide, the DM-associated DR molecules can be rapidly loaded and no longer bind to DM. Thus, DM seems to act as a dedicated class II-specific chaperone. In view of the suggested shortage of DM-resistant self-peptides in the loading compartment, empty class II molecules that are chaperoned by DM may enable the antigen-processing system to respond promptly to the challenge by newly entering antigens.

journal_name

Immunity

journal_title

Immunity

authors

Kropshofer H,Arndt SO,Moldenhauer G,Hämmerling GJ,Vogt AB

doi

10.1016/s1074-7613(00)80332-5

subject

Has Abstract

pub_date

1997-03-01 00:00:00

pages

293-302

issue

3

eissn

1074-7613

issn

1097-4180

pii

S1074-7613(00)80332-5

journal_volume

6

pub_type

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