Suppression of MHC class I surface expression by calreticulin's P-domain in a calreticulin deficient cell line

Changzhen Liu, Hongmei Fu, Barry Flutter, Simon J. Powis, Bin Gao

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

Calreticulin (CRT) is an important chaperone protein, comprising an N-domain, P-domain and C-domain. It is involved in the folding and assembly of multi-component protein complexes in the endoplasmic reticulum, and plays a critical role in MHC class I antigen processing and presentation. To dissect the functional role and molecular basis of individual domains of the protein, we have utilized individual domains to rescue impaired protein assembly in a CRT deficient cell line. Unexpectedly, both P-domain fragment and NP domain of CRT not only failed to rescue defective cell surface expression of MHC class I molecules but further inhibited their appearance on the surface of cells. Formation of the TAP-associated peptide-loading complex and trafficking of the few detectable MHC class I molecules were not significantly impaired. Instead, this further suppression of MHC class I molecules on the cell surface appears due to the complex missing antigenic peptides, the third member of fully assembled MHC class I molecules. Therefore the P-domain of calreticulin appears to play a significant role in antigen presentation by MHC class I molecules. (C) 2010 Elsevier B.V. All rights reserved.

Original languageEnglish
Pages (from-to)544-552
Number of pages9
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1803
Issue number5
DOIs
Publication statusPublished - May 2010

Keywords

  • MHC class I
  • Calreticulin
  • P-domain
  • MAJOR HISTOCOMPATIBILITY COMPLEX
  • PEPTIDE-LOADING COMPLEX
  • ENDOPLASMIC-RETICULUM
  • T-CELL
  • MOLECULAR CHAPERONE
  • CALNEXIN
  • TAPASIN
  • PROTEIN
  • ERP57
  • TRANSPORTER

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