Evidence map›Paper›PMID 27237050›Full record

ArticleMolecular cell2016

E3-Independent Constitutive Monoubiquitination Complements Histone Methyltransferase Activity of SETDB1.

Lidong Sun, Jia Fang

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. The Many Faces of SetDB1.Epigenomes · 2026
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Clr4Nature communications · 2024
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Monoubiquitination in Homeostasis and Cancer.International journal of molecular sciences · 2022
    Review
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

2 authors at 1 institution in 1 country.

Lidong SunDepartment of Tumor Biology, H. Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612, USA.
Jia FangDepartment of Tumor Biology, H. Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612, USA. Electronic address: Jia.Fang@moffitt.org.
Moffitt Cancer Center · US

Funding

MPP8-Mediated Epigenetic Network and Its Roles in Tumor ProgressionR01CA172774 · NCI · ROSWELL PARK CANCER INSTITUTE CORP · PI FANG, JIA · 2014 to 2018
$1.8M
NCI NIH HHS R01 CA172774
6 · The paper itself

Abstract

Ubiquitination typically occurs through the sequential action of three enzymes catalyzing ubiquitin activation (E1), conjugation (E2), and ligation (E3) and regulates diverse eukaryotic cellular processes. Although monoubiquitination commonly confers nondegradative activities, mechanisms underlying its temporal and spatial regulation and functional plasticity still remain largely unknown. Here we demonstrate that SETDB1, a major histone H3K9 methyltransferase is monoubiquitinated at the evolutionarily conserved lysine-867 in its SET-Insertion domain. This ubiquitination is directly catalyzed by UBE2E family of E2 enzymes in an E3-independent manner while the conjugated-ubiquitin (Ub) is protected from active deubiquitination. The resulting constitutive lysine-867 monoubiquitination is essential for SETDB1's enzymatic activity and endogenous retrovirus silencing in murine embryonic stem cells. Furthermore, the canonical hydrophobic patch on the conjugated-Ub is critical for Ub protection and function. Together, our findings highlight an E3-independent mechanism for monoubiquitination and reveal mechanistic details of SETDB1's enzymatic activity and the functional significance of its SET-Insertion.

Indexed as

DNA MethylationUbiquitinationAmino Acid MotifsAnimalsCatalysisCRISPR-Cas SystemsEmbryonic Stem CellsEndogenous RetrovirusesGene SilencingHEK293 CellsHeLa CellsHistone-Lysine N-MethyltransferaseHistonesHumansHydrophobic and Hydrophilic InteractionsLysineHistone-Lysine N-MethyltransferaseHistonesLysineProtein MethyltransferasesSETDB1 protein, humanSETDB1 protein, mouseUbiquitin-Conjugating Enzymes

Identifiers

PMID27237050
PMCPMC5346476
OpenAlexW2405470874

What OpenQuestion holds

Textmetadata
LicenceTDM
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.