Evidence map›Paper›PMID 25059663›Full record

ArticleThe Journal of biological chemistry2014

TIF1γ protein regulates epithelial-mesenchymal transition by operating as a small ubiquitin-like modifier (SUMO) E3 ligase for the transcriptional regulator SnoN1.

Yoshiho Ikeuchi, Shorafidinkhuja Dadakhujaev, Amrita S Chandhoke, Mai Anh Huynh, Anna Oldenborg, Mikako Ikeuchi, Lili Deng, Eric J Bennett, J Wade Harper, Azad Bonni and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Cancer-Associated Dysregulation of Sumo Regulators: Proteases and Ligases.International journal of molecular sciences · 2022
    Review
  6. The Role of SUMO E3 Ligases in Signaling Pathway of Cancer Cells.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The Transcriptional Regulator SnoN Promotes the Proliferation of Cerebellar Granule Neuron Precursors in the Postnatal Mouse Brain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  13. The Roles of TIF1γ in Cancer.Frontiers in oncology · 2019
    Review
  14. Review
  15. Article
  16. SUMO and the robustness of cancer.Nature reviews. Cancer · 2017
    Review
  17. Review
  18. Article
  19. The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1γ sumoylation and poly-SUMO chain elongation.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

11 authors at 4 institutions in 3 countries.

Yoshiho IkeuchiFrom the Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110, the Departments of Neurobiology and.
Shorafidinkhuja Dadakhujaevthe Southern Alberta Cancer Research Institute and Department of Biochemistry and Molecular Biology, Cumming School of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada.
Amrita S Chandhokethe Southern Alberta Cancer Research Institute and Department of Biochemistry and Molecular Biology, Cumming School of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada.
Mai Anh Huynhthe Departments of Neurobiology and.
Anna OldenborgFrom the Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110.
Mikako Ikeuchithe Departments of Neurobiology and.
Lili Dengthe Southern Alberta Cancer Research Institute and Department of Biochemistry and Molecular Biology, Cumming School of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada.
Eric J BennettCell Biology, Harvard Medical School, Boston, Massachusetts 02115, and.
J Wade HarperCell Biology, Harvard Medical School, Boston, Massachusetts 02115, and.
Azad BonniFrom the Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110, the Departments of Neurobiology and sbonni@ucalgary.ca.
Shirin Bonnithe Southern Alberta Cancer Research Institute and Department of Biochemistry and Molecular Biology, Cumming School of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada sbonni@ucalgary.ca.
University of Calgary · CAHarvard University · USInstitute of Neurobiology · BGWashington University in St. Louis · US

Funding

Medical Scientist Training ProgramT32GM007753 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WALENSKY, LOREN DAVID · 1985 to 2021
$50.0M
Ubiquitin Mediated Proteolysis and Cell Cycle ControlR01AG011085 · NIA · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JEFFREY W HARPER · 1993 to 2026
$10.9M
SIGNAL TRANSDUCTION PATHWAYS REGULATING NEURON SURVIVALR01NS041021 · NINDS · WASHINGTON UNIVERSITY · PI GABEL, HARRISON W · 2001 to 2023
$7.7M
CIHRNIA NIH HHS AG011085NIA NIH HHS R01 AG011085NIGMS NIH HHS T32 GM007753NINDS NIH HHS NS041021NINDS NIH HHS R01 NS041021
6 · The paper itself

Abstract

Epithelial-mesenchymal transition (EMT) is a fundamental cellular process that contributes to epithelial tissue morphogenesis during normal development and in tumor invasiveness and metastasis. The transcriptional regulator SnoN robustly influences EMT in response to the cytokine TGFβ, but the mechanisms that regulate the fundamental role of SnoN in TGFβ-induced EMT are not completely understood. Here we employ interaction proteomics to uncover the signaling protein TIF1γ as a specific interactor of SnoN1 but not the closely related isoform SnoN2. A 16-amino acid peptide within a unique region of SnoN1 mediates the interaction of SnoN1 with TIF1γ. Strikingly, although TIF1γ is thought to act as a ubiquitin E3 ligase, we find that TIF1γ operates as a small ubiquitin-like modifier (SUMO) E3 ligase that promotes the sumoylation of SnoN1 at distinct lysine residues. Importantly, TIF1γ-induced sumoylation is required for the ability of SnoN1 to suppress TGFβ-induced EMT, as assayed by the disruption of the morphogenesis of acini in a physiologically relevant three-dimensional model of normal murine mammary gland (NMuMG) epithelial cells. Collectively, our findings define a novel TIF1γ-SnoN1 sumoylation pathway that plays a critical role in EMT and has important implications for our understanding of TGFβ signaling and diverse biological processes in normal development and cancer biology.

Indexed as

Amino Acid SequenceAnimalsBinding SitesBlotting, WesternCell Culture TechniquesCell LineEpithelial CellsEpithelial-Mesenchymal TransitionGene ExpressionHEK293 CellsHep G2 CellsHumansIntracellular Signaling Peptides and ProteinsMammary Glands, AnimalMiceMicroscopy, FluorescenceIntracellular Signaling Peptides and ProteinsProto-Oncogene ProteinsSKIL protein, humanTranscription FactorsTransforming Growth Factor betaTRIM33 protein, humanUbiquitin-Protein LigasesCell SignalingEpithelial-Mesenchymal Transition (EMT)Protein-Protein InteractionSnoNSumoylationTIF1γTransforming Growth Factor β (TGFβ)

Identifiers

PMID25059663
PMCPMC4155673
OpenAlexW1993449328

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.