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Editorial
. 2021 Sep 13;1(3):100056.
doi: 10.1016/j.xops.2021.100056. eCollection 2021 Sep.

EnRAPtured: Is Endoplasmic Reticulum Aminopeptidase a New Clue to the Pathogenesis and ThERAPy of Uveitis?

James T Rosenbaum  1 , Tejpal Gill  1 , Tammy M Martin  1
Affiliations
Editorial

EnRAPtured: Is Endoplasmic Reticulum Aminopeptidase a New Clue to the Pathogenesis and ThERAPy of Uveitis?

James T Rosenbaum et al. Ophthalmol Sci. .
No abstract available

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Figures

Figure 1
Figure 1
Diagram showing the role of endoplasmic reticulum aminopeptidase (ERAP) in major histocompatibility complex (MHC) class I antigen processing and presentation. Exogenous proteins are digested into smaller peptides by the proteasome in the cytoplasm. These peptides are then translocated into the endoplasmic reticulum by transporter associated with antigen processing (TAP) proteins, where they undergo N-terminus trimming in the soluble or MHC bound form, by ERAP1, ERAP2, or both. The resulting peptide–MHC class I complex leaves the endoplasmic reticulum to reach cell surface via the Golgi complex. This peptide–MHC class I complex then binds to the T-cell receptor (TCR) and initiates antigen-specific response in CD8+ T cells.
See this image and copyright information in PMC

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