Evidence map›Paper›PMID 26903513›Full record

ArticleThe Journal of biological chemistry2016

Major Histocompatibility Complex (MHC) Class I Processing of the NY-ESO-1 Antigen Is Regulated by Rpn10 and Rpn13 Proteins and Immunoproteasomes following Non-lysine Ubiquitination.

Richard Golnik, Andrea Lehmann, Peter-Michael Kloetzel, Frédéric Ebstein

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Thioester and Oxyester Linkages in the Ubiquitin System.Methods in molecular biology (Clifton, N.J.) · 2023
    Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Varied Role of Ubiquitylation in Generating MHC Class I Peptide Ligands.Journal of immunology (Baltimore, Md. : 1950) · 2017
    Article
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Richard GolnikFrom the Institute for Biochemistry, Charité-Universitätsmedizin Berlin, Charité Platz 1/Virchowweg 6, 10117 Berlin, Germany.
Andrea LehmannFrom the Institute for Biochemistry, Charité-Universitätsmedizin Berlin, Charité Platz 1/Virchowweg 6, 10117 Berlin, Germany.
Peter-Michael KloetzelFrom the Institute for Biochemistry, Charité-Universitätsmedizin Berlin, Charité Platz 1/Virchowweg 6, 10117 Berlin, Germany.
Frédéric EbsteinFrom the Institute for Biochemistry, Charité-Universitätsmedizin Berlin, Charité Platz 1/Virchowweg 6, 10117 Berlin, Germany frederic.ebstein@charite.de.
Charité - Universitätsmedizin Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The supply of MHC class I-restricted peptides is primarily ensured by the degradation of intracellular proteins via the ubiquitin-proteasome system. Depending on the target and the enzymes involved, ubiquitination is a process that may dramatically vary in terms of linkages, length, and attachment sites. Here we identified the unique lysine residue at position 124 of the NY-ESO-1 cancer/testis antigen as the acceptor site for the formation of canonical Lys-48-linkages. Interestingly, a lysine-less form of NY-ESO-1 was as efficient as its wild-type counterpart in supplying the HLA-A*0201-restricted NY-ESO-1157-165 antigenic peptide. In fact, we show that the regulation of NY-ESO-1 processing by the ubiquitin receptors Rpn10 and Rpn13 as a well as by the standard and immunoproteasome is governed by non-canonical ubiquitination on non-lysine sites. In summary, our data underscore the significance of atypical ubiquitination in the modulation of MHC class I antigen processing.

Indexed as

Antigen PresentationAntigens, NeoplasmHeLa CellsHLA-A2 AntigenHumansIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMembrane ProteinsProteasome Endopeptidase ComplexRNA-Binding ProteinsUbiquitinationADRM1 protein, humanAntigens, NeoplasmCTAG1B protein, humanHLA-A*02:01 antigenHLA-A2 AntigenIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMembrane ProteinsProteasome Endopeptidase ComplexPSMD4 protein, humanRNA-Binding Proteinsantigen processingproteasomeprotein degradationtumor immunologyubiquitin

Identifiers

PMID26903513
PMCPMC4861448
OpenAlexW2337624445

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.