Calreticulin binds to the α1 domain of MHC class I independently of tapasin

H. R. Turnquist, S. E. Vargas, M. M. McIlhaney, S. Li, P. Wang, J. C. Solheim

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

Prior to binding to antigenic peptide, the major histocompatibility complex (MHC) heavy chain associates with an assembly complex of proteins that includes calreticulin, tapasin, and the transporter associated with antigen processing (TAP). Our data show that calreticulin can bind weakly to Ld without tapasin's assistance, and that deglycosylation of the α1 domain results in a primary loss of binding to calreticulin rather than tapasin. We have also shown that high amounts of wild-type tapasin are still unable to associate with MHC class I in the absence of the MHC class I/calreticulin interaction, confirming the central role of calreticulin in the formation of the MHC class I assembly complex.

Original languageEnglish (US)
Pages (from-to)18-24
Number of pages7
JournalTissue Antigens
Volume59
Issue number1
DOIs
StatePublished - 2002

Keywords

  • Antigen presentation
  • Calreticulin
  • Chaperone
  • Glycosylation
  • MHC class I
  • Tapasin

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Biochemistry
  • Genetics

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