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

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.

SUBMITTER: Howe C 

PROVIDER: S-EPMC2790484 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature

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

Howe Christopher C   Garstka Malgorzata M   Al-Balushi Mohammed M   Ghanem Esther E   Antoniou Antony N AN   Fritzsche Susanne S   Jankevicius Gytis G   Kontouli Nasia N   Schneeweiss Clemens C   Williams Anthony A   Elliott Tim T   Springer Sebastian S  

The EMBO journal 20091022 23

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 pe  ...[more]

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