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Chaperones and folding of MHC class I molecules in the endoplasmic reticulum.

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Author

Summary, in English

In this review we discuss the influence of chaperones on the general phenomena of folding as well as on the specific folding of an individual protein, MHC class I. MHC class I maturation is a highly sophisticated process in which the folding machinery of the endoplasmic reticulum (ER) is heavily involved. Understanding the MHC class I maturation per se is important since peptides loaded onto MHC class I molecules are the base for antigen presentation generating immune responses against virus, intracellular bacteria as well as tumours. This review discusses the early stages of MHC class I maturation regarding BiP and calnexin association, and differences in MHC class I heavy chain (HC) interaction with calnexin and calreticulin are highlighted. Late stage MHC class I maturation with focus on the dedicated chaperone tapasin is also discussed. (C) 2003 Elsevier Science B.V. All rights reserved.

Publishing year

2003

Language

English

Pages

1-12

Publication/Series

Biochimica et Biophysica Acta

Volume

1641

Issue

1

Document type

Journal article review

Publisher

Elsevier

Topic

  • Cell and Molecular Biology

Keywords

  • chaperone
  • tapasin
  • endoplasmic reticulum (ER)
  • MEC class I
  • folding

Status

Published

Research group

  • Antigen Presentation

ISBN/ISSN/Other

  • ISSN: 0006-3002