| Literature DB >> 20833720 |
Nicole L Glosson1, Patrick Gonyo, Nathan A May, Christine L Schneider, Laura C Ristow, Qiuhong Wang, Amy W Hudson.
Abstract
The U21 open reading frame from human herpesvirus-7 encodes a membrane protein that associates with and redirects class I MHC molecules to the lysosomal compartment. The mechanism by which U21 accomplishes this trafficking excursion is unknown. Here we have examined the contribution of localization, glycosylation, domain structure, and the absence of substrate class I MHC molecules on the ability of U21 to traffic to lysosomes. Our results suggest the existence of a cellular protein necessary for U21-mediated rerouting of class I MHC molecules.Entities:
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Year: 2010 PMID: 20833720 PMCID: PMC2978630 DOI: 10.1074/jbc.M110.125849
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157