Evidence map›Paper›PMID 24704831›Full record

ArticleOncogene2015

SUMOylation regulates AKT1 activity.

C F de la Cruz-Herrera, M Campagna, V Lang, J del Carmen González-Santamaría, L Marcos-Villar, M S Rodríguez, A Vidal, M Collado, C Rivas

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

32 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Review
  3. AKT kinases as therapeutic targets.Journal of experimental & clinical cancer research : CR · 2024
    Review
  4. Review
  5. SUMO modifies GβL and mediates mTOR signaling.The Journal of biological chemistry · 2024
    Article
  6. Article
  7. Review
  8. Article
  9. Targeting Akt in cancer for precision therapy.Journal of hematology & oncology · 2021
    Review
  10. Review
  11. Article
  12. SUMOylation modulates the stability and function of PI3K-p110β.Cellular and molecular life sciences : CMLS · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Inhibitors in AKTion: ATP-competitive vs allosteric.Biochemical Society transactions · 2020
    Review
  17. Article
  18. Article
  19. Review
  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

9 authors at 3 institutions in 1 country.

C F de la Cruz-HerreraDepartment of Molecular and Cellular Biology, Centro Nacional de Biotecnología-CSIC, Madrid, Spain.
M CampagnaDepartment of Molecular and Cellular Biology, Centro Nacional de Biotecnología-CSIC, Madrid, Spain.
V LangUbiquitylation and Cancer Molecular Biology laboratory, Inbiomed, San Sebastian-Donostia, Gipuzkoa, Spain.
J del Carmen González-SantamaríaDepartment of Molecular and Cellular Biology, Centro Nacional de Biotecnología-CSIC, Madrid, Spain.
L Marcos-VillarDepartment of Molecular and Cellular Biology, Centro Nacional de Biotecnología-CSIC, Madrid, Spain.
M S RodríguezUbiquitylation and Cancer Molecular Biology laboratory, Inbiomed, San Sebastian-Donostia, Gipuzkoa, Spain.
A VidalDepartamento de Fisioloxía and Centro de Investigación en Medicina Molecular (CIMUS), Universidade de Santiago de Compostela, Instituto de Investigaciones Sanitarias (IDIS), Santiago de Compostela, Spain.
M ColladoInstituto de Investigación Sanitaria de Santiago de Compostela (IDIS), Complexo Hospitalario Universitario de Santiago de Compostela (CHUS), SERGAS, Santiago de Compostela, Spain.
C Rivas1] Department of Molecular and Cellular Biology, Centro Nacional de Biotecnología-CSIC, Madrid, Spain [2] Centro de Investigación en Medicina Molecular (CIMUS), Universidade de Santiago de Compostela, Instituto de Investigaciones Sanitarias (IDIS), Santiago de Compostela, Spain.
Centro Nacional de Biotecnología · ESInstituto de Investigación Sanitaria de Santiago · ESUniversidade de Santiago de Compostela · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Serine threonine kinase AKT has a central role in the cell, controlling survival, proliferation, metabolism and angiogenesis. Deregulation of its activity underlies a wide range of pathological situations, including cancer. Here we show that AKT is post-translationally modified by the small ubiquitin-like modifier (SUMO) protein. Interestingly, neither SUMO conjugation nor activation of SUMOylated AKT is regulated by the classical AKT targeting to the cell membrane or by the phosphoinositide 3-kinase pathway. We demonstrate that SUMO induces the activation of AKT, whereas, conversely, down-modulation of the SUMO machinery diminishes AKT activation and cell proliferation. Furthermore, an AKT SUMOylation mutant shows reduced activation, and decreased anti-apoptotic and pro-tumoral activities in comparison with the wild-type protein. These results identify SUMO as a novel key regulator of AKT phosphorylation and activity.

Indexed as

3T3 CellsAnimalsApoptosisCell Line, TumorCell ProliferationChlorocebus aethiopsCOS CellsEnzyme ActivationFemaleHEK293 CellsHeLa CellsHumansMCF-7 CellsMiceMutationNeoplasmsAKT1 protein, humanPhosphoinositide-3 Kinase InhibitorsProto-Oncogene Proteins c-aktSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO1 protein, humanSUMO2 protein, humanSUMO3 protein, humanUbiquitins

Identifiers

PMID24704831
OpenAlexW1989360436

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.