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

Turnquist, HR; Vargas, SE; McIlhaney, MM; Li, Su-Ling LU ; Wang, P and Solheim, JC (2002) In Tissue Antigens 59(1). p.18-24
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.
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, calreticulin, MHC class I, antigen presentation, glycosylation
in
Tissue Antigens
volume
59
issue
1
pages
18 - 24
publisher
Wiley-Blackwell
external identifiers
  • wos:000175235700004
  • pmid:11972874
  • scopus:0036005673
ISSN
0001-2815
DOI
10.1034/j.1399-0039.2002.590104.x
language
English
LU publication?
yes
id
a55cad47-14b0-4223-8835-6a0ede647556 (old id 338751)
date added to LUP
2007-11-19 08:25:18
date last changed
2017-11-15 14:17:21
@article{a55cad47-14b0-4223-8835-6a0ede647556,
  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.},
  author       = {Turnquist, HR and Vargas, SE and McIlhaney, MM and Li, Su-Ling and Wang, P and Solheim, JC},
  issn         = {0001-2815},
  keyword      = {chaperone,tapasin,calreticulin,MHC class I,antigen presentation,glycosylation},
  language     = {eng},
  number       = {1},
  pages        = {18--24},
  publisher    = {Wiley-Blackwell},
  series       = {Tissue Antigens},
  title        = {Calreticulin binds to the alpha 1 domain of MHC class I independently of tapasin},
  url          = {http://dx.doi.org/10.1034/j.1399-0039.2002.590104.x},
  volume       = {59},
  year         = {2002},
}