Evidence map›Paper›PMID 21220452›Full record

ArticleThe Journal of experimental medicine2011

CD83 increases MHC II and CD86 on dendritic cells by opposing IL-10-driven MARCH1-mediated ubiquitination and degradation.

Lina E Tze, Keisuke Horikawa, Heather Domaschenz, Debbie R Howard, Carla M Roots, Robert J Rigby, David A Way, Mari Ohmura-Hoshino, Satoshi Ishido, Christopher E Andoniou and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

140 citing papers in PubMed, 221 citations in OpenAlex.

  1. Developing Antiviral Vaccines Based on AttenuatedPathogens (Basel, Switzerland) · 2026
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  8. USP35 Acts as a Deubiquitinating Enzyme for ID3 to Promote Immune Escape in Colorectal Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
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  16. CD83 suppresses endogenous March-I-dependent MHC class II ubiquitination, endocytosis, and degradation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article

80 more citing papers are in PubMed but not listed here.

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

12 authors at 4 institutions in 2 countries.

Lina E TzeImmunology Department, John Curtin School of Medical Research, the Australian National University, Canberra ACT 2601, Australia.
Keisuke Horikawa
Heather Domaschenz
Debbie R Howard
Carla M Roots
Robert J Rigby
David A Way
Mari Ohmura-Hoshino
Satoshi Ishido
Christopher E Andoniou
Mariapia A Degli-Esposti
Christopher C Goodnow
Australian National University · AURIKEN Center for Integrative Medical Sciences · JPLions Eye Institute · AUUniversity of Western Australia · AU

Funding

Wellcome Trust
6 · The paper itself

Abstract

Effective vaccine adjuvants must induce expression of major histocompatibility (MHC) class II proteins and the costimulatory molecule CD86 on dendritic cells (DCs). However, some adjuvants elicit production of cytokines resulting in adverse inflammatory consequences. Development of agents that selectively increase MHC class II and CD86 expression without triggering unwanted cytokine production requires a better understanding of the molecular mechanisms influencing the production and degradation of MHC class II and CD86 in DCs. Here, we investigate how CD83, an immunoglobulin protein expressed on the surface of mature DCs, promotes MHC class II and CD86 expression. Using mice with an N-ethyl-N-nitrosourea-induced mutation eliminating the transmembrane (TM) region of CD83, we found that the TM domain of CD83 enhances MHC class II and CD86 expression by blocking MHC class II association with the ubiquitin ligase MARCH1. The TM region of CD83 blocks interleukin 10-driven, MARCH1-dependent ubiquitination and degradation of MHC class II and CD86 in DCs. Exploiting this posttranslational pathway for boosting MHC class II and CD86 expression on DCs may provide an opportunity to enhance the immunogenicity of vaccines.

Indexed as

UbiquitinationAmino Acid SequenceAnimalsAntigens, CDB7-2 AntigenBase SequenceCD83 AntigenCell MembraneDendritic CellsHEK293 CellsHistocompatibility Antigens Class IIHumansImmunoglobulinsInterleukin-10MaleMembrane GlycoproteinsAntigens, CDB7-2 AntigenCD83 AntigenCd86 protein, mouseHistocompatibility Antigens Class IIImmunoglobulinsInterleukin-10MARCH1 protein, mouseMembrane GlycoproteinsUbiquitin-Protein Ligases

Identifiers

PMID21220452
PMCPMC3023131
OpenAlexW2160375521

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.