Journal
EMBO JOURNAL
Volume 28, Issue 23, Pages 3730-3744Publisher
WILEY
DOI: 10.1038/emboj.2009.296
Keywords
calreticulin; endoplasmic reticulum; major histocompatibility complex (MHC) class I molecules; peptides; quality control
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Funding
- Cancer Research UK
- Deutsche Forschungsgemeinschaft [SP 583/2]
- German Academic Exchange Service (DAAD)
- EMBO
- Sultan Qaboos University
- Jacobs University
- Arthritis Career Development Fellowship [18440]
- Versus Arthritis [18440] Funding Source: researchfish
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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. The EMBO Journal (2009) 28, 3730-3744. doi: 10.1038/emboj.2009.296; Published online 22 October 2009
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