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. 2011 Oct 13;7(10):e1002144. doi: 10.1371/journal.pcbi.1002144

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Dalchau et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Degradation of cytosolic and nuclear proteins, predominantly by the proteasome, generates peptides that are actively transported into the lumen of the endoplasmic reticulum (ER). Loading and editing of peptide cargo on MHC class I is achieved in the peptide loading complex, resulting in loaded MHC class I being released into the Golgi and transported to the cell surface, where the MHC class I peptide complex is presented to the immune system via the T-cell receptor. Known constituents of the peptide loading complex such as the transporter for antigen processing (TAP), tapasin, ERp57, calreticulin and MHC heavy-chain together with are shown explicitly.

Inline graphic — Degradation of cytosolic and nuclear proteins, predominantly by the proteasome, generates peptides that are actively transported into the lumen of the endoplasmic reticulum (ER). Loading and editing of peptide cargo on MHC class I is achieved in the peptide loading complex, resulting in loaded MHC class I being released into the Golgi and transported to the cell surface, where the MHC class I peptide complex is presented to the immune system via the T-cell receptor. Known constituents of the peptide loading complex such as the transporter for antigen processing (TAP), tapasin, ERp57, calreticulin and MHC heavy-chain together with are shown explicitly.