Comparative analysis of the impact of a free cysteine in tapasin on the maturation and surface expression of murine MHC class i allotypes: Short Communication

X. Wang, L. C. Simone, A. Tuli, Joyce C Solheim

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2 Citations (Scopus)

Abstract

Tapasin is a key molecule in the major histocompatibility complex (MHC) class I peptide-loading complex, interacting with several other proteins in the complex. An amino acid substitution at a free cysteine position in tapasin has been shown to disrupt the covalent association of tapasin with ERp57. In this study, we mutated the free cysteine in mouse tapasin, and analysed the effects on the cell surface expression of the mouse MHC class I molecules Kd and Kb. The C95S substitution in mouse tapasin increased the proportion of open forms relative to folded forms for both types of MHC class I molecules at the cell surface. Furthermore, the C95S substitution resulted in increased association of tapasin with folded Kd. Overall, our studies with these mouse MHC class I allotypes have revealed that the free cysteine 95 in mouse tapasin influences stable expression at the plasma membrane for both MHC class I allotypes, and have shown that tapasin's interaction with folded Kd is elevated by the C95S substitution in tapasin.

Original languageEnglish (US)
Pages (from-to)183-187
Number of pages5
JournalInternational Journal of Immunogenetics
Volume36
Issue number3
DOIs
StatePublished - Jun 1 2009

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Major Histocompatibility Complex
Cysteine
Communication
tapasin
Amino Acid Substitution
Cell Membrane
Peptides

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology
  • Genetics
  • Genetics(clinical)

Cite this

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title = "Comparative analysis of the impact of a free cysteine in tapasin on the maturation and surface expression of murine MHC class i allotypes: Short Communication",
abstract = "Tapasin is a key molecule in the major histocompatibility complex (MHC) class I peptide-loading complex, interacting with several other proteins in the complex. An amino acid substitution at a free cysteine position in tapasin has been shown to disrupt the covalent association of tapasin with ERp57. In this study, we mutated the free cysteine in mouse tapasin, and analysed the effects on the cell surface expression of the mouse MHC class I molecules Kd and Kb. The C95S substitution in mouse tapasin increased the proportion of open forms relative to folded forms for both types of MHC class I molecules at the cell surface. Furthermore, the C95S substitution resulted in increased association of tapasin with folded Kd. Overall, our studies with these mouse MHC class I allotypes have revealed that the free cysteine 95 in mouse tapasin influences stable expression at the plasma membrane for both MHC class I allotypes, and have shown that tapasin's interaction with folded Kd is elevated by the C95S substitution in tapasin.",
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AU - Wang, X.

AU - Simone, L. C.

AU - Tuli, A.

AU - Solheim, Joyce C

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N2 - Tapasin is a key molecule in the major histocompatibility complex (MHC) class I peptide-loading complex, interacting with several other proteins in the complex. An amino acid substitution at a free cysteine position in tapasin has been shown to disrupt the covalent association of tapasin with ERp57. In this study, we mutated the free cysteine in mouse tapasin, and analysed the effects on the cell surface expression of the mouse MHC class I molecules Kd and Kb. The C95S substitution in mouse tapasin increased the proportion of open forms relative to folded forms for both types of MHC class I molecules at the cell surface. Furthermore, the C95S substitution resulted in increased association of tapasin with folded Kd. Overall, our studies with these mouse MHC class I allotypes have revealed that the free cysteine 95 in mouse tapasin influences stable expression at the plasma membrane for both MHC class I allotypes, and have shown that tapasin's interaction with folded Kd is elevated by the C95S substitution in tapasin.

AB - Tapasin is a key molecule in the major histocompatibility complex (MHC) class I peptide-loading complex, interacting with several other proteins in the complex. An amino acid substitution at a free cysteine position in tapasin has been shown to disrupt the covalent association of tapasin with ERp57. In this study, we mutated the free cysteine in mouse tapasin, and analysed the effects on the cell surface expression of the mouse MHC class I molecules Kd and Kb. The C95S substitution in mouse tapasin increased the proportion of open forms relative to folded forms for both types of MHC class I molecules at the cell surface. Furthermore, the C95S substitution resulted in increased association of tapasin with folded Kd. Overall, our studies with these mouse MHC class I allotypes have revealed that the free cysteine 95 in mouse tapasin influences stable expression at the plasma membrane for both MHC class I allotypes, and have shown that tapasin's interaction with folded Kd is elevated by the C95S substitution in tapasin.

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