{"doi":"10.1073/pnas.93.24.13997","title":"Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin–class I–TAP complexes","abstract":"<jats:p>\n                    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 β\n                    <jats:sub>2</jats:sub>\n                    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.\n                  </jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1996,"id":679516,"datarank":0.6628260911694899,"base_score":4.418840607796598,"endowment":4.418840607796598,"self_citation_contribution":0.6628260911694899,"citation_network_contribution":0.0,"self_endowment_contribution":0.6628260911694899,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":82,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1775418,"name":"Kelly P. Kearse","orcid":null,"position":1,"is_corresponding":false},{"id":1775416,"name":"Jeroen E. M. Van Leeuwen","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin–class I–TAP complexes","abstract":"<jats:p>\n                    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 β\n                    <jats:sub>2</jats:sub>\n                    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.\n                  </jats:p>","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"8943049","pmcid":"PMC19483","openalex_id":null,"authors":[],"funders":[],"total_grants":0,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"green","license":null,"oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/19483","host_type":"repository"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.93.24.13997","host_type":"publisher"}],"fields_of_study":["ATP Binding Cassette Transporter, Subfamily B, Member 2","ATP-Binding Cassette Transporters","Animals","Antibodies","Autoantigens","Calcium-Binding Proteins","Calnexin","Calreticulin","Endoplasmic Reticulum","Glycosylation","H-2 Antigens","Kinetics","Mice","Mice, Inbred C57BL","Protein Binding","Ribonucleoproteins","Spleen","T-Lymphocytes"],"mesh_terms":["Spleen","T-Lymphocytes","Endoplasmic Reticulum","Animals","Mice, Inbred C57BL","Mice","Calcium-Binding Proteins","Calnexin","Calreticulin","ATP-Binding Cassette Transporters","Ribonucleoproteins","Antibodies","H-2 Antigens","Autoantigens","Protein Binding","Glycosylation","Kinetics","ATP Binding Cassette Transporter, Subfamily B, Member 2"],"keywords":[],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-17T13:19:11.467057Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}