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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)
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author
publishing date
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
2009-07-10 11:50:45
date last changed
2016-11-18 10:39:37
@misc{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    = {ARRAY(0xb897078)},
  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},
  volume       = {176},
  year         = {2006},
}