The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a “molecular ruler” mechanism
Open accessAbstract
Endoplasmic reticulum aminopeptidase 1 (ERAP1) is an IFN-γ-induced aminopeptidase in the endoplasmic reticulum that trims longer precursors to the antigenic peptides presented on MHC class I molecules. We recently reported that purified ERAP1 trimmed N-extended precursors but spared peptides of 8-9 residues, the length required for binding to MHC class I molecules. Here, we show another remarkable property of ERAP1: that it strongly prefers substrates 9-16 residues long, the lengths of peptides transported efficiently into the ER by the transporter associated with antigen processing (TAP) transporter. This aminopeptidase rapidly degraded a model 13-mer to a 9-mer and then stopped, even though the substrate and the product had identical N- and C-terminal sequences. No other aminopeptidase, including the closely related ER-aminopeptidase ERAP2, showed a similar length preference. Unlike other aminopeptidases, the activity of ERAP1 depended on the C-terminal residue of the substrate. ERAP1, like most MHC class I molecules, prefers peptides with hydrophobic C termini and shows low affinity for peptides with charged C termini. Thus, ERAP1 is specialized to process precursors transported by TAP to peptides that can serve as MHC class I epitopes. Its “molecular ruler” mechanism involves binding the hydrophobic C terminus of the substrate 9-16 residues away from the active site.
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Self-citationAn IFN-γ–induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I–presented peptides
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Towards a systems understanding of MHC class I and MHC class II antigen presentation
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Association scan of 14,500 nonsynonymous SNPs in four diseases identifies autoimmunity variants
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Present yourself! by MHC class I and MHC class II molecules
Rock, K. L., Reits, E., & Neefjes, J. (2016) · Trends in Immunology · doi:10.1016/j.it.2016.08.010 · Cited by 814
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Metadata
- Authors
- Chang, S.-C., Momburg, F., Bhutani, N., & Goldberg, A. L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-11-14
- Volume
- 102
- Issue
- 47
- Pages
- 17107-17112
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2042689290
- Cited by
- 326
- References
- 43
- FWCI
- 3.69
- Type
- journal article
- Language
- en
- Open access
- green
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- Chang, S.-C., Momburg, F., Bhutani, N., & Goldberg, A. L. (2005). The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a “molecular ruler” mechanism. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0500721102
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