Open AccessDeglucosylation of N-linked glycans is an important step in the dissociation of calreticulin–class I–TAP complexes
Author(s) -
Jeroen E.M. van Leeuwen,
Kelly P. Kearse
Publication year - 1996
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.93.24.13997
Subject(s) - calnexin , calreticulin , transporter associated with antigen processing , endoplasmic reticulum , mhc class i , glycan , biology , microbiology and biotechnology , antigen processing , major histocompatibility complex , chaperone (clinical) , glycoprotein , chemistry , biochemistry , gene , medicine , pathology
Recent evidence indicates that newly synthesized major histocompatibility complex (MHC) class I proteins interact with calnexin, a transmembrane endoplasmic reticulum protein specific for certain glycoproteins bearing monoglucosylated glycans. Here, we studied the association of newly synthesized class I proteins with calreticulin, a soluble calnexin-related ER protein, in murine T cells. We found that, unlike calnexin–class I interactions, calreticulin assembly with class I proteins was markedly decreased in the absence of β2 microglobulin expression and that calreticulin associated with a subset of class I glycoforms distinct from those assembled with calnexin but similar to those bound to TAP (transporter associated with antigen processing) proteins. Finally, these studies show that deglucosylation of N-linked glycans is important for dissociation of class I proteins from both calreticulin and TAP and that the vast majority of newly synthesized class I proteins associated with calreticulin are simultaneously assembled with TAP. The data demonstrate that calnexin and calreticulin chaperones assemble with distinct MHC class I assembly intermediates in the ER and show that glycan processing is functionally coupled to release of MHC class I proteins from peptide transport molecules.