Cited by 482vaccines and immunoinformatics approachesPeptidase Inhibition and AnalysisImmunotherapy and Immune Responses

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Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum

Saveanu, Loredana, Carroll, Oliver, Lindo, Vivian, Del Val, Margarita, Lopez, Daniel, Lepelletier, Yves, Greer, Fiona, Schomburg, Lutz, Fruci, Doriana, Niedermann, Gabriele, van Endert, Peter M·2005·Nature Immunology

DOI 10.1038/ni1208

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Abstract

The generation of many HLA class I peptides entails a final trimming step in the endoplasmic reticulum that, in humans, is accomplished by two 'candidate' aminopeptidases. We show here that one of these, ERAP1, was unable to remove several N-terminal amino acids that were trimmed efficiently by the second enzyme, ERAP2. This trimming of a longer peptide required the concerted action of both ERAP1 and ERAP2, both for in vitro digestion and in vivo for cellular antigen presentation. ERAP1 and ERAP2 localized together in vivo and associated physically in complexes that were most likely heterodimeric. Thus, the human endoplasmic reticulum is equipped with a pair of trimming aminopeptidases that have complementary functions in HLA class I peptide presentation.

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A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids.
Wessel, D., & Flügge, U. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90782-6 · Cited by 3,997
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DEGRADATION OF CELL PROTEINS AND THE GENERATION OF MHC CLASS I-PRESENTED PEPTIDES
Rock, K. L., & Goldberg, A. L. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.739 · Cited by 923
ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum
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A viral inhibitor of peptide transporters for antigen presentation
Früh, K., Ahn, K., Djaballah, H., Sempé, P., Endert, P. V., Tampé, R., Peterson, P. A., & Yang, Y. M. (1995) · Nature · doi:10.1038/375415a0 · Cited by 601
An IFN-γ–induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I–presented peptides
Šarić, T., Chang, S., Hattori, A., York, I. A., Markant, S. L., Rock, K. L., Tsujimoto, M., & Goldberg, A. L. (2002) · Nature Immunology · doi:10.1038/ni859 · Cited by 532
The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8–9 residues
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Current Protocols in Cell Biology
Bonifacino, J. S., Dasso, M., Harford, J. B., Lippincott‐Schwartz, J., & Yamada, K. M. (2001) · John Wiley & Sons, Inc. eBooks · doi:10.1002/0471143030 · Cited by 509
Producing Nature’s Gene-Chips: The Generation of Peptides for Display by MHC Class I Molecules
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Endert, P. V., Tampé, R., Meyer, T. H., Tisch, R., Bach, J., & McDevitt, H. O. (1994) · Immunity · doi:10.1016/1074-7613(94)90091-4 · Cited by 287

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Authors: Saveanu, L., Carroll, O., Lindo, V., Del Val, M., Lopez, D., Lepelletier, Y., Greer, F., Schomburg, L., Fruci, D., Niedermann, G., & van Endert, P. M.
Affiliations: Inserm (FR)
Centre National de la Recherche Scientifique (FR)
Charité – Universitätsmedizin Berlin (DE)
Max Planck Society (DE)
ORCID: Saveanu, Loredana
Lepelletier, Yves
Schomburg, Lutz
Fruci, Doriana
Niedermann, Gabriele
Venue: Nature Immunology
Publisher: Springer Science and Business Media LLC
Published: 2005-05-22
Volume: 6
Issue: 7
Pages: 689-697
ISSN: 1529-2908 (ISSN-L)
1529-2916
DOI: 10.1038/ni1208
OpenAlex: W1981338942
Cited by: 481
References: 35
Citations by year: 2026: 8 · 2025: 18 · 2024: 18 · 2023: 31 · 2022: 20 · 2021: 23 · 2020: 28 · 2019: 30 · 2018: 25 · 2017: 25 · 2016: 15 · 2015: 26 · 2014: 25 · 2013: 31 · 2012: 27
FWCI: 7.65
Type: journal article
Language: en
Open access: closed
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Nature Immunology (publishedVersion)
PubMed (publishedVersion)
FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
Funders: Comunidad de Madrid
European Commission
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Peptidase Inhibition and Analysis
Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
Keywords: ERAP1, ERAP2, aminopeptidase, peptide trimming, HLA class I, endoplasmic reticulum, antigen presentation
MeSH terms: Aminopeptidases, Epitopes, Endoplasmic Reticulum, HeLa Cells, Humans, Microsomes, Peptide Fragments, RNA, Immunoblotting, Histocompatibility Antigens Class I, Minor Histocompatibility Antigens, Antigen Presentation, Reverse Transcriptase Polymerase Chain Reaction, RNA Interference

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Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum

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