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

Record type: Article

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.

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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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Published date: 2 December 2009
Organisations: Cancer Sciences


Local EPrints ID: 73282
ISSN: 0261-4189
PURE UUID: 88dfae00-a16c-40ad-be9c-65726ab7dc8d
ORCID for Tim Elliott: ORCID iD

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Date deposited: 04 Mar 2010
Last modified: 18 Jul 2017 23:50

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Author: Christopher Howe
Author: Malgorzata Garstka
Author: Mohammed Al-Balushi
Author: Esther Ghanem
Author: Antony N. Antoniou
Author: Susanne Fritzsche
Author: Gytis Jankevicius
Author: Nasia Kontouli
Author: Clemens Schneeweiss
Author: Sebastian Springer
Author: Tim Elliott ORCID iD

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