Department of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA.
J Biol Chem. 2010 Nov 19;285(47):37016-29. doi: 10.1074/jbc.M110.125849. Epub 2010 Sep 10.
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.
人类疱疹病毒 7 的 U21 开放阅读框编码一种膜蛋白，该蛋白与 I 类主要组织相容性复合体（MHC）分子结合，并将其重定向到溶酶体区室。U21 完成这种运输过程的机制尚不清楚。在这里，我们研究了定位、糖基化、结构域结构以及缺乏底物 I 类 MHC 分子对 U21 向溶酶体运输能力的贡献。我们的结果表明，存在一种细胞蛋白对于 U21 介导的 I 类 MHC 分子重定向是必需的。
