Calreticulin binds to the alpha 1 domain of MHC class I independently of tapasin

Research output: Contribution to journalArticle

Abstract

Prior to binding to antigenic peptide, the major histoconipatibility 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 L-d without tapasin's assistance, and that deglycosylation of the alpha1 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.

Details

Authors
  • HR Turnquist
  • SE Vargas
  • MM McIlhaney
  • Su-Ling Li
  • P Wang
  • JC Solheim
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Clinical Medicine

Keywords

  • chaperone, tapasin, calreticulin, MHC class I, antigen presentation, glycosylation
Original languageEnglish
Pages (from-to)18-24
JournalTissue Antigens
Volume59
Issue number1
Publication statusPublished - 2002
Publication categoryResearch
Peer-reviewedYes