Evidence map›Paper›PMID 34638625›Full record

ArticleInternational journal of molecular sciences2021

Regulation of O-Linked N-Acetyl Glucosamine Transferase (OGT) through E6 Stimulation of the Ubiquitin Ligase Activity of E6AP.

Kangli Peng, Ruochuan Liu, Caiwei Jia, Yiyang Wang, Geon H Jeong, Li Zhou, Ronggui Hu, Hiroaki Kiyokawa, Jun Yin, Bo Zhao

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. UBE4B Mediates Mitophagy via NIPSNAP1 Ubiquitination and NDP52 Recruitment.International journal of molecular sciences · 2026
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Insights into O-GlcNAcylation and programmed cell death in cancer.Frontiers in cell and developmental biology · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. 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

10 authors at 5 institutions in 2 countries.

Kangli PengEngineering Research Center of Cell and Therapeutic Antibody, Ministry of Education, School of Pharmacy, Shanghai Jiao Tong University, Shanghai 200240, China.ORCID 0000-0003-1361-2340
Ruochuan LiuDepartment of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
Caiwei JiaCenter for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai 100864, China.
Yiyang WangDepartment of Pathophysiology, School of Medicine, Jinan University, Guangzhou 510632, China.
Geon H JeongDepartment of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
Li ZhouDepartment of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
Ronggui HuCenter for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai 100864, China.
Hiroaki KiyokawaDepartment of Pharmacology, Northwestern University, Chicago, IL 60611, USA.ORCID 0000-0002-7942-6455
Jun YinDepartment of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
Bo ZhaoEngineering Research Center of Cell and Therapeutic Antibody, Ministry of Education, School of Pharmacy, Shanghai Jiao Tong University, Shanghai 200240, China.ORCID 0000-0001-7188-5959
Georgia State University · USChinese Academy of Sciences · CNJinan University · CNNorthwestern University · USShanghai Jiao Tong University · CN

Funding

Orthogonal Ubiquitin Transfer to Profile E3 Substrate Specificity.R01GM104498 · NIGMS · UNIVERSITY OF CHICAGO · PI KIYOKAWA, HIROAKI, YIN, JUN · 2013 to 2021
$3.2M
National Natural Science Foundation of China 31770921;31971187National Science Foundation 1710460; 2109051NIGMS NIH HHS R01 GM104498NIH HHS R01GM104498Science and Technology Commission of Shanghai Municipality Project 20JC1411200
6 · The paper itself

Abstract

Glycosyltransferase OGT catalyzes the conjugation of O-linked β-D-N-acetylglucosamine (O-GlcNAc) to Ser and Thr residues of the cellular proteins and regulates many key processes in the cell. Here, we report the identification of OGT as a ubiquitination target of HECT-type E3 ubiquitin (UB) ligase E6AP, whose overexpression in HEK293 cells would induce the degradation of OGT. We also found that the expression of E6AP in HeLa cells with the endogenous expression of the E6 protein of the human papillomavirus (HPV) would accelerate OGT degradation by the proteasome and suppress O-GlcNAc modification of OGT substrates in the cell. Overall, our study establishes a new mechanism of OGT regulation by the ubiquitin-proteasome system (UPS) that mediates the crosstalk between protein ubiquitination and O-GlcNAcylation pathways underlying diverse cellular processes.

Indexed as

Cell LineCell Line, TumorHEK293 CellsHeLa CellsHumansN-AcetylglucosaminyltransferasesOncogene Proteins, ViralPapillomaviridaeProteasome Endopeptidase ComplexUbiquitinUbiquitinationUbiquitin-Protein LigasesN-AcetylglucosaminyltransferasesOGT protein, humanOncogene Proteins, ViralProteasome Endopeptidase ComplexUBE3A protein, humanUbiquitinUbiquitin-Protein LigasesE6E6APhuman papillomavirusO-GlcNAcO-GlcNAcylationOGTubiquitinubiquitination

Identifiers

PMID34638625
PMCPMC8508608
OpenAlexW3204820096

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.