Evidence map›Paper›PMID 27326929›Full record

ArticleDevelopmental cell2016

Stuxnet Facilitates the Degradation of Polycomb Protein during Development.

Juan Du, Junzheng Zhang, Tao He, Yajuan Li, Ying Su, Feng Tie, Min Liu, Peter J Harte, Alan Jian Zhu

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Structure of the TXNL1-bound proteasome.Nature structural & molecular biology · 2025
    Article
  4. Degrons: defining the rules of protein degradation.Nature reviews. Molecular cell biology · 2025
    Review
  5. Article
  6. Article
  7. Structural insights into the ubiquitin-independent midnolin-proteasome pathway.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Life science alliance · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Ubiquitin proteasome system in circadian rhythm and sleep homeostasis: Lessons from Drosophila.Genes to cells : devoted to molecular & cellular mechanisms · 2022
    Review
  15. Article
  16. Article
  17. Article
  18. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

Juan DuState Key Laboratory of Membrane Biology, Ministry of Education Key Laboratory of Cell Proliferation and Differentiation, School of Life Sciences, Peking University, Beijing 100871, China; Peking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, China.
Junzheng ZhangState Key Laboratory of Membrane Biology, Ministry of Education Key Laboratory of Cell Proliferation and Differentiation, School of Life Sciences, Peking University, Beijing 100871, China; Peking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, China.
Tao HeState Key Laboratory of Membrane Biology, Ministry of Education Key Laboratory of Cell Proliferation and Differentiation, School of Life Sciences, Peking University, Beijing 100871, China.
Yajuan LiState Key Laboratory of Membrane Biology, Ministry of Education Key Laboratory of Cell Proliferation and Differentiation, School of Life Sciences, Peking University, Beijing 100871, China.
Ying SuState Key Laboratory of Membrane Biology, Ministry of Education Key Laboratory of Cell Proliferation and Differentiation, School of Life Sciences, Peking University, Beijing 100871, China.
Feng TieDepartment of Genetics and Genome Sciences, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Min LiuState Key Laboratory of Membrane Biology, Ministry of Education Key Laboratory of Cell Proliferation and Differentiation, School of Life Sciences, Peking University, Beijing 100871, China; Peking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, China.
Peter J HarteDepartment of Genetics and Genome Sciences, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Alan Jian ZhuState Key Laboratory of Membrane Biology, Ministry of Education Key Laboratory of Cell Proliferation and Differentiation, School of Life Sciences, Peking University, Beijing 100871, China; Peking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, China. Electronic address: zhua@pku.edu.cn.
State Key Laboratory of Membrane BiologyPeking University · CNCase Western Reserve University · USUniversity School · US

Funding

MOLECULAR BASIS OF HOMEOTIC GENE REGULATIONR01GM039255 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI HARTE, PETER J. · 1988 to 2020
$7.1M
Reversible phosphorylation in Hedgehog signalingR01GM085175 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI ZHU, ALAN · 2009 to 2013
$1.5M
NIGMS NIH HHS R01 GM039255NIGMS NIH HHS R01 GM085175
6 · The paper itself

Abstract

Polycomb-group (PcG) proteins function to ensure correct deployment of developmental programs by epigenetically repressing target gene expression. Despite the importance, few studies have been focused on the regulation of PcG activity itself. Here, we report a Drosophila gene, stuxnet (stx), that controls Pc protein stability. We find that heightened stx activity leads to homeotic transformation, reduced Pc activity, and de-repression of PcG targets. Conversely, stx mutants, which can be rescued by decreased Pc expression, display developmental defects resembling hyperactivation of Pc. Our biochemical analyses provide a mechanistic basis for the interaction between stx and Pc; Stx facilitates Pc degradation in the proteasome, independent of ubiquitin modification. Furthermore, this mode of regulation is conserved in vertebrates. Mouse stx promotes degradation of Cbx4, an orthologous Pc protein, in vertebrate cells and induces homeotic transformation in Drosophila. Our results highlight an evolutionarily conserved mechanism of regulated protein degradation on PcG homeostasis and epigenetic activity.

Indexed as

ProteolysisAmino Acid SequenceAnimalsConserved SequenceDrosophila melanogasterDrosophila ProteinsEpistasis, GeneticPolycomb Repressive Complex 1Proteasome Endopeptidase ComplexProtein BindingProtein DomainsStructure-Activity RelationshipUbiquitinationVertebratesDrosophila ProteinsPc protein, DrosophilaPolycomb Repressive Complex 1Proteasome Endopeptidase ComplexStx protein, Drosophila

Identifiers

PMID27326929
PMCPMC7365346
OpenAlexW2471019167

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.