Calreticulin binds to the alpha 1 domain of MHC class I independently of tapasin
(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:
https://lup.lub.lu.se/record/338751
- author
- Turnquist, HR ; Vargas, SE ; McIlhaney, MM ; Li, Su-Ling LU ; Wang, P and Solheim, JC
- organization
- publishing date
- 2002
- 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
- 2016-04-01 16:52:27
- date last changed
- 2022-03-22 21:46:18
@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}}, keywords = {{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}}, doi = {{10.1034/j.1399-0039.2002.590104.x}}, volume = {{59}}, year = {{2002}}, }