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

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-7282-5 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-7283-3
Genre: Journal Article

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Ortmann, B., Author
Copeman, J., Author
Lehner, P. J., Author
Sadasivan, B., Author
Herberg, J. A., Author
Grandea, A. G., Author
Riddell, S. R., Author
Tampe, R.1, Author
Spies, T., Author
Trowsdale, J., Author
Cresswell, P., Author
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1External Organizations, ou_persistent22              

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Free keywords: Hla class-i; Peptide-binding; Antigen presentation; Cell line; Molecules; Transporters; Expression; Retention; Pathway; Charge.; Multidisciplinary. Multidisciplinary. Multidisciplinary.
 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]

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 Dates: 1997-08-29
 Publication Status: Issued
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 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 318696
DOI: 10.1126/science.277.5330.1306
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Title: Science
Source Genre: Journal
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Pages: - Volume / Issue: 277 (5330) Sequence Number: - Start / End Page: 1306 - 1309 Identifier: -