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A critical role for tapasin in the assembly and function of multimeric mhc class i-tap complexes

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Ortmann, B., Copeman, J., Lehner, P. J., Sadasivan, B., Herberg, J. A., Grandea, A. G., et al. (1997). A critical role for tapasin in the assembly and function of multimeric mhc class i-tap complexes. Science, 277(5330), 1306-1309. doi:10.1126/science.277.5330.1306.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-7282-5
Abstract
Newly assembled major histocompatibility complex (MHC) class I molecules, together with the endoplasmic reticulum chaperone calreticulin, interact with the transporter associated with antigen processing (TAP) through a molecule called tapasin, The molecular cloning of tapasin revealed it to be a transmembrane glycoprotein encoded by an MHC-linked gene. It is a member of the immunoglobulin superfamily with a probable cytoplasmic endoplasmic reticulum retention signal. Up to four MHC class I-tapasin complexes were found to bind to each TAP molecule. Expression of tapasin in a negative mutant human cell line (220) restored class I-TAP association and normal class I cell surface expression. Tapasin expression also corrected the defective recognition of virus-infected 220 cells by class I-restricted cytotoxic T cells, establishing a critical functional role for tapasin in MHC class I-restricted antigen processing. [References: 38]