Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum

被引:50
作者
Paulsson, KM
Kleijmeer, MJ
Griffith, J
Jevon, M
Chen, SW
Anderson, PO
Sjögren, HO
Li, SL
Wang, P
机构
[1] Lund Univ, Inst Tumor Immunol, S-22362 Lund, Sweden
[2] Univ Med Ctr, Inst Biomembranes, Dept Cell Biol, NL-3584 CX Utrecht, Netherlands
[3] Brunel Univ, Dept Biol Sci, Uxbridge UB8 3PH, Middx, England
[4] Barts & London Sch Med & Dent, Dept Gastroenterol, Immunol Grp, London EC1A 7ED, England
关键词
D O I
10.1074/jbc.M201388200
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
Tapasin is a subunit of the transporter associated with antigen processing (TAP). It associates with the major histocompatibility complex (MHC) class I. We show that tapasin interacts with beta- and gamma-subunits of COPI coatomer. COPI retrieves membrane proteins from the Golgi network back to the endoplasmic reticulum (ER). The COPI subunit-associated tapasin also interacts with MHC class I molecules suggesting that tapasin acts as the cargo receptor for packing MHC class I molecules as cargo proteins into COPI-coated vesicles. In tapasin mutant cells, neither TAP nor MHC class I are detected in association with the COPI coatomer. Interestingly, tapasin-associated MHC class I molecules are antigenic peptide-receptive and detected in both the ER and the Golgi. Our data suggest that tapasin is required for the COPI vesicle-mediated retrograde transport of immature MHC class I molecules from the Golgi network to the ER.
引用
收藏
页码:18266 / 18271
页数:6
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