Retention of empty MHC class I molecules by tapasin is essential to reconstitute antigen presentation in invertebrate cells

Gary J. Schoenhals, R. Murli Krishna, Andres G. Grandea, Thomas Spies, Per A. Peterson, Young Yang, Klaus Früh

Research output: Contribution to journalArticle

92 Scopus citations

Abstract

Presentation of antigen-derived peptides by major histocompatibility complex (MHC) class I molecules is dependent on an endoplasmic reticulum (ER) resident glycoprotein, tapasin, which mediates their interaction with the transporter associated with antigen processing (TAP). Independently of TAP, tapasin was required for the presentation of peptides targeted to the ER by signal sequences in MHC class I-transfected insect cells. Tapasin increased MHC class I peptide loading by retaining empty but not peptide-containing MHC class I molecules in the ER. Upon co-expression of TAP, this retention/release function of tapasin was sufficient to reconstitute MHC class I antigen presentation in insect cells, thus defining the minimal non-housekeeping functions required for MHC class I antigen presentation.

Original languageEnglish (US)
Pages (from-to)743-753
Number of pages11
JournalEMBO Journal
Volume18
Issue number3
DOIs
StatePublished - Feb 1 1999

Keywords

  • Antigen presentation
  • Chaperone
  • MHC
  • Proteasome
  • Transpsrter associated with antigen processing

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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