Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules


Howe, Christopher, Garstka, Malgorzata, Al-Balushi, Mohammed, Ghanem, Esther, Antoniou, Antony N., Fritzsche, Susanne, Jankevicius, Gytis, Kontouli, Nasia, Schneeweiss, Clemens, Williams, Anthony, Springer, Sebastian and Elliott, Tim (2009) Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules The EMBO Journal, 28, (23), pp. 3730-3744. (doi:10.1038/emboj.2009.296).

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Description/Abstract

Calreticulin is a lectin chaperone of the endoplasmic reticulum (ER). In calreticulin-deficient cells, major histocompatibility complex (MHC) class I molecules travel to the cell surface in association with a sub-optimal peptide load. Here, we show that calreticulin exits the ER to accumulate in the ER–Golgi intermediate compartment (ERGIC) and the cis-Golgi, together with sub-optimally loaded class I molecules. Calreticulin that lacks its C-terminal KDEL retrieval sequence assembles with the peptide-loading complex but neither retrieves sub-optimally loaded class I molecules from the cis-Golgi to the ER, nor supports optimal peptide loading. Our study, to the best of our knowledge, demonstrates for the first time a functional role of intracellular transport in the optimal loading of MHC class I molecules with antigenic peptide.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1038/emboj.2009.296
ISSNs: 0261-4189 (print)
Subjects: R Medicine > RC Internal medicine > RC0254 Neoplasms. Tumors. Oncology (including Cancer)
ePrint ID: 73282
Date :
Date Event
2 December 2009Published
Date Deposited: 04 Mar 2010
Last Modified: 24 Feb 2017 10:43
Projects:
UNSPECIFIED
Funded by: CRUK (UNSPECIFIED)
UNSPECIFIED to UNSPECIFIED
Further Information:Google Scholar
URI: http://eprints.soton.ac.uk/id/eprint/73282

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