Evidence map›Paper›PMID 17502423›Full record

ArticleThe Journal of cell biology2007

Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3.

Xiaoli Wang, Roger A Herr, Wei-Jen Chua, Lonnie Lybarger, Emmanuel J H J Wiertz, Ted H Hansen

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 174 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
174citing papers in PubMed, 1 pooled it
9.9field-weighted citation impact, top 1% 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

174 citing papers in PubMed, 1 synthesis or guideline pooled it, 309 citations in OpenAlex.

  1. Pooled it
  2. Review
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  5. Article
  6. Article
  7. Review
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  10. Article
  11. Article
  12. Insights into non-proteinaceous ubiquitination.Biochemical Society transactions · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. The Ubiquitin Tale: Current Strategies and Future Challenges.ACS pharmacology & translational science · 2024
    Review
  17. Article
  18. Review
  19. Article
  20. Review

114 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

6 authors at 3 institutions in 2 countries.

Xiaoli WangDepartment of Pathology and Immunology, Washington University School of Medicine, St Louis, MO 63110, USA.
Roger A Herr
Wei-Jen Chua
Lonnie Lybarger
Emmanuel J H J Wiertz
Ted H Hansen
Washington University in St. Louis · USLeiden University Medical Center · NLUniversity of Arizona · US

Funding

MHC-I regulation by herpes virusR01AI019687 · NIAID · WASHINGTON UNIVERSITY · PI FREMONT, DAVED H. · 1985 to 2016
$5.2M
Ubiquitin-mediated pathways of viral immune evasionR01AI060723 · NIAID · UNIVERSITY OF ARIZONA · PI LYBARGER, LONNIE P · 2004 to 2008
$1.7M
NIAID NIH HHS AI19687NIAID NIH HHS AI60723NIAID NIH HHS R01 AI019687NIAID NIH HHS R01 AI060723
6 · The paper itself

Abstract

The mechanism by which substrates for endoplasmic reticulum-associated degradation are retrotranslocated to the cytosol remains largely unknown, although ubiquitination is known to play a key role. The mouse gamma-herpesvirus protein mK3 is a viral RING-CH-type E3 ligase that specifically targets nascent major histocompatibility complex I heavy chain (HC) for degradation, thus blocking the immune detection of virus-infected cells. To address the question of how HC is retrotranslocated and what role mK3 ligase plays in this action, we investigated ubiquitin conjugation sites on HC using mutagenesis and biochemistry approaches. In total, our data demonstrate that mK3-mediated ubiquitination can occur via serine, threonine, or lysine residues on the HC tail, each of which is sufficient to induce the rapid degradation of HC. Given that mK3 has numerous cellular and viral homologues, it will be of considerable interest to determine the pervasiveness of this novel mechanism of ubiquitination.

Indexed as

Amino Acid SequenceAnimalsCell LineCytoplasmEndoplasmic ReticulumGammaherpesvirinaeHistocompatibility Antigens Class IHumansLysineMiceMice, Inbred C57BLMolecular Sequence DataProtein Structure, TertiarySerineThreonineUbiquitinHistocompatibility Antigens Class ILysineSerineThreonineUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID17502423
PMCPMC2064207
OpenAlexW2058209707

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.