Evidence map›Paper›PMID 22713753›Full record

ArticleNature communications2012

SUMO1 modification of PTEN regulates tumorigenesis by controlling its association with the plasma membrane.

Jian Huang, Jie Yan, Jian Zhang, Shiguo Zhu, Yanli Wang, Ting Shi, Changhong Zhu, Cheng Chen, Xin Liu, Jinke Cheng and 4 more

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 133 papers.

0numbers the graph read from it
0cells of the map it votes in
133citing papers in PubMed
9.0field-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

133 citing papers in PubMed, 203 citations in OpenAlex.

  1. Article
  2. PTEN Subcellular Localization Dictates Function.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. The role of SUMOylation in epithelial-mesenchymal transition.Journal of molecular medicine (Berlin, Germany) · 2025
    Review
  9. Article
  10. Article
  11. The impact of dysregulation SUMOylation on prostate cancer.Journal of translational medicine · 2025
    Review
  12. Article
  13. The therapeutic potential of RNA m(6)A in lung cancer.Cell communication and signaling : CCS · 2024
    Review
  14. Article
  15. Article
  16. Article
  17. SUMO modifies GβL and mediates mTOR signaling.The Journal of biological chemistry · 2024
    Article
  18. Article
  19. N4-acetylcytidine modifies primary microRNAs for processing in cancer cells.Cellular and molecular life sciences : CMLS · 2024
    Article
  20. Review

73 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

14 authors at 5 institutions in 3 countries.

Jian HuangDepartment of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-SM), Shanghai 200025, China.
Jie Yan
Jian Zhang
Shiguo Zhu
Yanli Wang
Ting Shi
Changhong Zhu
Cheng Chen
Xin Liu
Jinke Cheng
Tomas Mustelin
Gen-Sheng Feng
Guoqiang Chen
Jianxiu Yu
Shanghai Jiao Tong University · CNShanghai Cancer Institute · CNMinistry of Education · THSanford Burnham Prebys Medical Discovery Institute · USUniversity of California, San Diego · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The membrane association of the tumour suppressor phosphatase and tensin homologue (PTEN) is required to oppose the phosphatidylinositol-3-kinase/AKT pathway by dephosphorylation of phosphatidylinositol-3,4,5-triphosphate (PIP3). How cytosolic PTEN interacts with its main substrate, PIP3, localized at the inner face of plasma membrane remains unclear. Here we show that PTEN is covalently modified by SUMO1 at both K(266) and K(254) sites in the C2 domain of PTEN. SUMO1 modification at K(266) located in the CBR3 loop, which has a central role in PTEN membrane association, mainly facilitates cooperative binding of PTEN to the plasma membrane by electrostatic interactions. This results in the downregulation of the phosphatidylinositol-3 kinase/AKT pathway and consequently, suppression of anchorage-independent cell proliferation and tumour growth in vivo. Our data demonstrate a molecular mechanism whereby SUMO1 modification is required for PTEN tumour suppressor function by controlling PTEN membrane association and regulation of the phosphatidylinositol-3 kinase/AKT pathway.

Indexed as

AnimalsCell LineCell MembraneCell Transformation, NeoplasticFluorescent Antibody TechniqueHeLa CellsHumansMaleMiceMicroscopy, ConfocalMolecular Dynamics SimulationProstatic NeoplasmsPTEN PhosphohydrolaseSUMO-1 ProteinXenograft Model Antitumor AssaysPTEN PhosphohydrolaseSUMO-1 ProteinSUMO1 protein, human

Identifiers

PMID22713753
OpenAlexW2168239981

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.