期刊
HUMAN IMMUNOLOGY
卷 76, 期 4, 页码 292-296出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.humimm.2015.02.002
关键词
Antigen presentation; COPII; NleA; Di-arginine; Invariant chain; MHC class II
类别
资金
- National Science and Engineering Research Council of Canada (NSERC) [2985371]
Four invariant chain (Ii) isoforms assist the folding and trafficking of human MHC class II (MHCIIs). The main isoforms, Iip33 and lip35, assemble in the ER into homo- and/or hetero-trimers. The sequential binding of up to three MHCII alpha beta heterodimers to Ii trimers results in the formation of pentamers, heptamers and nonamers. MHCIIs are required to overcome the p35-encoded di-arginine (RxR) ER retention motif and to allow anterograde trafficking of the complex. Here, we show that inactivation of the RxR motif requires a direct cis interaction between p35 and the MHCII, precluding ER egress of some unsaturated Ii trimers. Interestingly, as opposed to MHCII/p33 complexes, those including p35 remained in the ER when co-expressed with the NleA protein of enterohaemorrhagic Escherichia coil. Taken together, our results demonstrate that p35 influences distinctively MHCII/li assembly and trafficking. (C) 2015 American Society for Histocompatibility and Immunogenetics. Published by Elsevier Inc. All rights reserved.
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