ArticleThe Journal of biological chemistry2009
ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activity.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 55 citations in OpenAlex.
- Protein Disulfide Isomerase Endoplasmic Reticulum Protein 57 (ERp57) is Protective Against ALS-Associated Mutant TDP-43 in Neuronal Cells.Neuromolecular medicine · 2024Article
- In oxygen-deprived tumor cells ERp57 provides radioprotection and ensures proliferation via c-Myc, PLK1 and the AKT pathway.Scientific reports · 2021Article
- Calnexin cycle - structural features of the ER chaperone system.The FEBS journal · 2020Review
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- Article
- Molecular Chaperone Calnexin Regulates the Function ofFrontiers in molecular neuroscience · 2017Article
- Depletion of the thiol oxidoreductase ERp57 in tumor cells inhibits proliferation and increases sensitivity to ionizing radiation and chemotherapeutics.Oncotarget · 2015Article
- Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides.Molecular biology of the cell · 2015Article
- Transient covalent interactions of newly synthesized thyroglobulin with oxidoreductases of the endoplasmic reticulum.The Journal of biological chemistry · 2014Article
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- Stepwise assembly of fibrinogen is assisted by the endoplasmic reticulum lectin-chaperone system in HepG2 cells.PloS one · 2013Article
- Calreticulin in the immune system: ins and outs.Trends in immunology · 2013Review
- The disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosis.Blood · 2012Article
- ERp57/GRP58: a protein with multiple functions.Cellular & molecular biology letters · 2011Review
- Structural and functional relationships between the lectin and arm domains of calreticulin.The Journal of biological chemistry · 2011Article
- The Ca2+ pumps of the endoplasmic reticulum and Golgi apparatus.Cold Spring Harbor perspectives in biology · 2011Review
- Essential glycan-dependent interactions optimize MHC class I peptide loading.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The polypeptide binding conformation of calreticulin facilitates its cell-surface expression under conditions of endoplasmic reticulum stress.The Journal of biological chemistry · 2011Article
- Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.The Journal of biological chemistry · 2010Article
- Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins.Molecular biology of the cell · 2010Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
ERp57 is a thiol oxidoreductase that catalyzes disulfide formation in heavy chains of class I histocompatibility molecules. It also forms a mixed disulfide with tapasin within the class I peptide loading complex, stabilizing the complex and promoting efficient binding of peptides to class I molecules. Since ERp57 associates with the lectin chaperones calnexin and calreticulin, it is thought that ERp57 requires these chaperones to gain access to its substrates. To test this idea, we examined class I biogenesis in cells lacking calnexin or calreticulin or that express an ERp57 mutant that fails to bind to these chaperones. Remarkably, heavy chain disulfides formed at the same rate in these cells as in wild type cells. Moreover, ERp57 formed a mixed disulfide with tapasin and promoted efficient peptide loading in the absence of interactions with calnexin and calreticulin. These findings suggest that ERp57 has the capacity to recognize its substrates directly in addition to being recruited through lectin chaperones. We also found that calreticulin could be recruited into the peptide loading complex in the absence of interactions with both ERp57 and substrate oligosaccharides, demonstrating the importance of its polypeptide binding site in substrate recognition. Finally, by inactivating the redox-active sites of ERp57, we demonstrate that its enzymatic activity is dispensable in stabilizing the peptide loading complex and in supporting efficient peptide loading. Thus, ERp57 appears to play a structural rather than catalytic role within the peptide loading complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.