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International Immunology Advance Access originally published online on November 16, 2004
International Immunology 2005 17(1):45-53; doi:10.1093/intimm/dxh184
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© 2005 The Japanese Society for Immunology

Exogenous antigens are processed through the endoplasmic reticulum-associated degradation (ERAD) in cross-presentation by dendritic cells

Jun Imai1,2,3, Hironori Hasegawa1,4, Mikako Maruya1,2,3, Shigeo Koyasu1,2,3 and Ichiro Yahara1,2,3,4

1 Keio Research Park and 2 Department of Microbiology and Immunology, Keio University School of Medicine, Shinjuku-ku, Tokyo 160-8582, Japan
3 CREST, Japan Science and Technology Corporation, Kawaguchi 332-0012, Japan
4 Ina Institute, Medical & Biological Laboratories, Inc., Ltd, Ina-shi 396-0002, Japan

Correspondence to: I. Yahara; E-mail:iyahara{at}mbl.co.jp

Antigen cross-presentation is critical in infectious and tumor immunity where cytotoxic T lymphocytes are induced by dendritic cells specifically equipped with cellular machineries to present exogenous antigens with major histocompatibility complex (MHC) class I molecules. To examine molecular mechanisms of antigen cross-presentation, we employed as a model system a murine dendritic cell line DC2.4 capable of presenting soluble antigens such as ovalbumin (OVA) with MHC class I. Here, we demonstrate that exogenously added OVA is accumulated in the endoplasmic reticulum (ER) and late endosomes followed by retrograde transport to the cytoplasm through the Sec61 transporter complexes, and that CHIP functions as an E3 ubiquitin–ligase for OVA degradation by proteasomes. This mechanism is essentially the same as that known as the ER-associated degradation (ERAD) in the quality control of secretary and membrane proteins.

Keywords: CHIP, ovalbumin, RNAi, Sec61, VCP

Transmitting editor: T. Saito


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