Evidence map›Paper›PMID 21896490›Full record

ArticleThe Journal of biological chemistry2011

Ubiquitin-mediated regulation of CD86 protein expression by the ubiquitin ligase membrane-associated RING-CH-1 (MARCH1).

Kathleen Corcoran, Maurice Jabbour, Candida Bhagwandin, Martin J Deymier, Debra L Theisen, Lonnie Lybarger

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

49 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
  2. Article
  3. 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
  4. Article
  5. Article
  6. Curcumin Inhibits the Growth of Hepatocellular CarcinomaRecent patents on anti-cancer drug discovery · 2025
    Article
  7. Article
  8. Review
  9. Ubiquitin Signaling in the Immune System.Advances in experimental medicine and biology · 2024
    Review
  10. Role of Ubiquitin Signaling in Modulating Dendritic Cell Function.Advances in experimental medicine and biology · 2024
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

Kathleen CorcoranDepartment of Cellular and Molecular Medicine, University of Arizona, Tucson, Arizona 85721, USA.
Maurice Jabbour
Candida Bhagwandin
Martin J Deymier
Debra L Theisen
Lonnie Lybarger
University of Arizona · US

Funding

Ubiquitin-mediated pathways of viral immune evasionR01AI060723 · NIAID · UNIVERSITY OF ARIZONA · PI LYBARGER, LONNIE P · 2004 to 2008
$1.7M
UBIQUITIN-DEPENDENT REGULATION OF IMMUNE ACTIVATIONR56AI080756 · NIAID · UNIVERSITY OF ARIZONA · PI LYBARGER, LONNIE P · 2010 to 2010
$335k
NIAID NIH HHS AI060723NIAID NIH HHS AI080756NIAID NIH HHS R01 AI060723NIAID NIH HHS R56 AI080756
6 · The paper itself

Abstract

The activation of naïve T cells requires antigen presentation by dendritic cells (DCs), and the process of antigen presentation is regulated over the course of DC maturation. One key aspect of this regulation is the cell surface up-regulation upon DC maturation of peptide·MHC-II complexes and the costimulatory molecule CD86. It is now clear that these critical induction events involve changes in ubiquitin-dependent trafficking of MHC-II and CD86 by the E3 ligase membrane-associated RING-CH-1 (MARCH1). Although ubiquitin-dependent trafficking of MHC-II has been well characterized, much less is known regarding the post-transcriptional regulation of CD86 expression. Here, we examined the physical and functional interaction between CD86 and MARCH1. We observed that CD86 is rapidly endocytosed in the presence of MARCH1 followed by lysosome-dependent degradation. Furthermore, we found that the association between CD86 and MARCH1 was conferred primarily by the transmembrane domains of the respective proteins. In contrast to MHC-II, which has a single, conserved ubiquitin acceptor site in the cytosolic domain, we found that multiple lysine residues in the cytosolic tail of CD86 could support ubiquitination consistent with the relative lack of sequence conservation across species within the CD86 cytosolic domain. These findings suggest that MARCH1 recruits multiple substrates via transmembrane domain-mediated interactions to permit substrate ubiquitination in the face of diverse cytosolic domain sequences.

Indexed as

ProteolysisAnimalsB7-2 AntigenCell LineEndocytosisGene Expression RegulationLysosomesMiceMice, KnockoutProtein Structure, TertiaryUbiquitinUbiquitinationUbiquitin-Protein LigasesB7-2 AntigenCd86 protein, mouseMARCH1 protein, mouseUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID21896490
PMCPMC3199464
OpenAlexW2040633452

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.