The double lysine motif of tapasin is a retrieval signal for retention of unstable MHC class I molecules in the endoplasmic reticulum
Paulsson, Kajsa M LU
; Jevon, Marc
; Wang, James W
; Li, Suling
and Wang, Ping
(2006)
In Journal of Immunology
176(12).
p.7482-7488
- Abstract
- Tapasin (tpn), an essential component of the MHC class I (MHC I) loading complex, has a canonical double lysine motif acting as a retrieval signal, which mediates retrograde transport of escaped endoplasmic reticulum (ER) proteins from the Golgi back to the ER. In this study, we mutated tpn with a substitution of the double lysine motif to double alanine (GFP-tpn-aa). This mutation abolished interaction with the coatomer protein complex I coatomer and resulted in accumulation of GFP-tpn-aa in the Golgi compartment, suggesting that the double lysine is important for the retrograde transport of tpn from late secretory compartments to the ER. In association with the increased Golgi distribution, the amount of MHC I exported from the ER to the... (More)
- Tapasin (tpn), an essential component of the MHC class I (MHC I) loading complex, has a canonical double lysine motif acting as a retrieval signal, which mediates retrograde transport of escaped endoplasmic reticulum (ER) proteins from the Golgi back to the ER. In this study, we mutated tpn with a substitution of the double lysine motif to double alanine (GFP-tpn-aa). This mutation abolished interaction with the coatomer protein complex I coatomer and resulted in accumulation of GFP-tpn-aa in the Golgi compartment, suggesting that the double lysine is important for the retrograde transport of tpn from late secretory compartments to the ER. In association with the increased Golgi distribution, the amount of MHC I exported from the ER to the surface was increased in 721.220 cells transfected with GFP-tpn-aa. However, the expressed MHC I were less stable and had increased turnover rate. Our results suggest that tpn with intact double lysine retrieval signal regulates retrograde transport of unstable MHC I molecules from the Golgi back to the ER to control the quality of MHC I Ag presentation. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1298377
- author
- Paulsson, Kajsa M
LU
; Jevon, Marc
; Wang, James W
; Li, Suling
and Wang, Ping
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Immunology
- volume
- 176
- issue
- 12
- pages
- 7482 - 7488
- publisher
- American Association of Immunologists
- external identifiers
-
- wos:000238101800040
- scopus:33744936808
- ISSN
- 1550-6606
- language
- English
- LU publication?
- no
- id
- b9bff63e-2d6b-4f36-b968-1a8cd17c7e2c (old id 1298377)
- alternative location
- http://www.jimmunol.org/cgi/content/abstract/176/12/7482
- date added to LUP
- 2016-04-04 12:06:57
- date last changed
- 2022-04-24 01:44:52
@article{b9bff63e-2d6b-4f36-b968-1a8cd17c7e2c,
abstract = {{Tapasin (tpn), an essential component of the MHC class I (MHC I) loading complex, has a canonical double lysine motif acting as a retrieval signal, which mediates retrograde transport of escaped endoplasmic reticulum (ER) proteins from the Golgi back to the ER. In this study, we mutated tpn with a substitution of the double lysine motif to double alanine (GFP-tpn-aa). This mutation abolished interaction with the coatomer protein complex I coatomer and resulted in accumulation of GFP-tpn-aa in the Golgi compartment, suggesting that the double lysine is important for the retrograde transport of tpn from late secretory compartments to the ER. In association with the increased Golgi distribution, the amount of MHC I exported from the ER to the surface was increased in 721.220 cells transfected with GFP-tpn-aa. However, the expressed MHC I were less stable and had increased turnover rate. Our results suggest that tpn with intact double lysine retrieval signal regulates retrograde transport of unstable MHC I molecules from the Golgi back to the ER to control the quality of MHC I Ag presentation.}},
author = {{Paulsson, Kajsa M and Jevon, Marc and Wang, James W and Li, Suling and Wang, Ping}},
issn = {{1550-6606}},
language = {{eng}},
number = {{12}},
pages = {{7482--7488}},
publisher = {{American Association of Immunologists}},
series = {{Journal of Immunology}},
title = {{The double lysine motif of tapasin is a retrieval signal for retention of unstable MHC class I molecules in the endoplasmic reticulum}},
url = {{http://www.jimmunol.org/cgi/content/abstract/176/12/7482}},
volume = {{176}},
year = {{2006}},
}