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

Paulsson, Kajsa M LU and Wang, Ping (2003) In Biochimica et Biophysica Acta 1641(1). p.1-12
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
chaperone, tapasin, endoplasmic reticulum (ER), MEC class I, folding
in
Biochimica et Biophysica Acta
volume
1641
issue
1
pages
1 - 12
publisher
Elsevier
external identifiers
  • pmid:12788224
  • wos:000183481800001
  • scopus:0038697962
ISSN
0006-3002
DOI
language
English
LU publication?
yes
id
5c4be31f-046d-4d5f-abcd-3d63f4214fdb (old id 116118)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12788224&dopt=Abstract
date added to LUP
2007-07-18 15:48:18
date last changed
2018-05-29 12:03:42
@article{5c4be31f-046d-4d5f-abcd-3d63f4214fdb,
  abstract     = {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.},
  author       = {Paulsson, Kajsa M and Wang, Ping},
  issn         = {0006-3002},
  keyword      = {chaperone,tapasin,endoplasmic reticulum (ER),MEC class I,folding},
  language     = {eng},
  number       = {1},
  pages        = {1--12},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta},
  title        = {Chaperones and folding of MHC class I molecules in the endoplasmic reticulum.},
  url          = {http://dx.doi.org/},
  volume       = {1641},
  year         = {2003},
}