Retention of empty MHC class I molecules by tapasin is essential to reconstitute antigen presentation in invertebrate cells

被引:106
作者
Schoenhals, GJ
Krishna, RM
Grandea, AG
Spies, T
Peterson, PA
Yang, Y
Früh, K
机构
[1] RW Johnson Pharmaceut Res Inst, San Diego, CA 92121 USA
[2] Fred Hutchinson Canc Res Ctr, Div Clin Res, Seattle, WA 98104 USA
关键词
antigen presentation; chaperone; MHC; proteasome; transporter associated with antigen processing;
D O I
10.1093/emboj/18.3.743
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Presentation of antigen-derived peptides by major histocompatibility complex (MHC) class I molecules is dependent on an endoplasmic reticulum (ER) resident glycoprotein, tapasin, which mediates their interaction with the transporter associated with antigen processing (TAP), Independently of TAP, tapasin was required for the presentation of peptides targeted to the ER by signal sequences in MHC class I-transfected insect cells. Tapasin increased MHC class I peptide loading by retaining empty but not peptide-containing MHC class I molecules in the ER, Upon co-expression of TAP, this retention/release function of tapasin was sufficient to reconstitute MHC class I antigen presentation in insect cells, thus defining the minimal non-housekeeping functions required for MHC class I antigen presentation.
引用
收藏
页码:743 / 753
页数:11
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