{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Huang L"],"funding":["NIAID NIH HHS"],"pagination":["1634-44"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3102268"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["30(8)"],"pubmed_abstract":["The forces that drive conversion of nascent protein to major histocompatibility complex (MHC) class I-restricted peptides remain unknown. We explored the fundamental property of overt hydrophobicity as such a driver. Relocation of a membrane glycoprotein to the cytosol via signal sequence ablation resulted in rapid processing of nascent protein not because of the misfolded luminal domain but because of the unembedded transmembrane (TM) domain, which serves as a dose-dependent degradation motif. Dislocation of the TM domain during the natural process of endoplasmic reticulum-associated degradation (ERAD) similarly accelerated peptide production, but in the context of markedly prolonged processing that included nonnascent species. These insights into intracellular proteolytic pathways and th"],"journal":["The EMBO journal"],"pubmed_title":["Hydrophobicity as a driver of MHC class I antigen processing."],"pmcid":["PMC3102268"],"funding_grant_id":["AI39501","R01 AI039501"],"pubmed_authors":["Eisenlohr LC","Huang L","Kuhls MC"],"additional_accession":[]},"is_claimable":false,"name":"Hydrophobicity as a driver of MHC class I antigen processing.","description":"The forces that drive conversion of nascent protein to major histocompatibility complex (MHC) class I-restricted peptides remain unknown. We explored the fundamental property of overt hydrophobicity as such a driver. Relocation of a membrane glycoprotein to the cytosol via signal sequence ablation resulted in rapid processing of nascent protein not because of the misfolded luminal domain but because of the unembedded transmembrane (TM) domain, which serves as a dose-dependent degradation motif. Dislocation of the TM domain during the natural process of endoplasmic reticulum-associated degradation (ERAD) similarly accelerated peptide production, but in the context of markedly prolonged processing that included nonnascent species. These insights into intracellular proteolytic pathways and th","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Apr","modification":"2025-04-18T13:59:58.419Z","creation":"2019-03-27T00:42:00Z"},"accession":"S-EPMC3102268","cross_references":{"pubmed":["21378750"],"doi":["10.1038/emboj.2011.62"]}}