Evidence map›Paper›PMID 26411363›Full record

ArticleOncogene2016

Conjugation of SUMO to p85 leads to a novel mechanism of PI3K regulation.

C F de la Cruz-Herrera, M Baz-Martínez, V Lang, A El Motiam, J Barbazán, R Couceiro, M Abal, A Vidal, M Esteban, C Muñoz-Fontela and 4 more

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2016. 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
0.6field-weighted citation impact, top 30% 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, 26 citations in OpenAlex.

  1. The role of SUMOylation in epithelial-mesenchymal transition.Journal of molecular medicine (Berlin, Germany) · 2025
    Review
  2. Free energy landscape of the PI3Kα C-terminal activation.Computational and structural biotechnology journal · 2024
    Article
  3. Review
  4. The Role of PIK3R1 in Metabolic Function and Insulin Sensitivity.International journal of molecular sciences · 2023
    Review
  5. Review
  6. Pathological Mechanism and Targeted Drugs of COPD.International journal of chronic obstructive pulmonary disease · 2022
    Review
  7. The orchestrated signaling by PI3Kα and PTEN at the membrane interface.Computational and structural biotechnology journal · 2022
    Review
  8. Review
  9. Article
  10. Article
  11. SUMOylation modulates the stability and function of PI3K-p110β.Cellular and molecular life sciences : CMLS · 2021
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. 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

14 authors at 5 institutions in 2 countries.

C F de la Cruz-HerreraDepartmento de Biología Molecular y Celular, Centro Nacional de Biotecnología-CSIC, Darwin 3, Madrid, Spain.
M Baz-MartínezCentro de Investigación en Medicina Molecular y Enfermedades Crónicas (CIMUS), Universidade de Santiago de Compostela, Instituto de Investigaciones Sanitarias (IDIS), Santiago de Compostela, Spain.
V LangUbiquitylation and Cancer Molecular Biology Laboratory, Inbiomed, San Sebastian-Donostia, Gipuzkoa, Spain.
A El MotiamCentro de Investigación en Medicina Molecular y Enfermedades Crónicas (CIMUS), Universidade de Santiago de Compostela, Instituto de Investigaciones Sanitarias (IDIS), Santiago de Compostela, Spain.
J BarbazánInstituto de Investigación Sanitaria de Santiago de Compostela (IDIS), Complexo Hospitalario Universitario de Santiago de Compostela (CHUS), SERGAS, Santiago de Compostela, Spain.
R CouceiroInstituto de Investigación Sanitaria de Santiago de Compostela (IDIS), Complexo Hospitalario Universitario de Santiago de Compostela (CHUS), SERGAS, Santiago de Compostela, Spain.
M AbalInstituto de Investigación Sanitaria de Santiago de Compostela (IDIS), Complexo Hospitalario Universitario de Santiago de Compostela (CHUS), SERGAS, Santiago de Compostela, Spain.
A VidalCentro de Investigación en Medicina Molecular y Enfermedades Crónicas (CIMUS), Universidade de Santiago de Compostela, Instituto de Investigaciones Sanitarias (IDIS), Santiago de Compostela, Spain.
M EstebanDepartmento de Biología Molecular y Celular, Centro Nacional de Biotecnología-CSIC, Darwin 3, Madrid, Spain.
C Muñoz-FontelaHeinrich Pette Institute, Leibniz Institute for Experimental Virology, Hamburg, Germany.
A NietoDepartmento de Biología Molecular y Celular, Centro Nacional de Biotecnología-CSIC, Darwin 3, Madrid, Spain.
M S RodríguezUbiquitylation and Cancer Molecular Biology Laboratory, Inbiomed, San Sebastian-Donostia, Gipuzkoa, 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 RivasDepartmento de Biología Molecular y Celular, Centro Nacional de Biotecnología-CSIC, Darwin 3, Madrid, Spain.
Instituto de Investigación Sanitaria de Santiago · ESCentro Nacional de Biotecnología · ESComplexo Hospitalario Universitario A Coruña · ESLeibniz Institute of Virology (LIV) · DEServicio Gallego de Salud · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Class IA phosphatidylinositol 3-kinases (PI3Ks) are composed of p110 catalytic and p85 regulatory subunits. How regulatory subunits modulate PI3K activity remains only partially understood. Here we identified SUMO (small ubiquitin-related modifier) as a new player modulating this regulation. We demonstrate that both p85β and p85α are conjugated to SUMO1 and SUMO2. We identified two lysine residues located at the inter-SH2 domain on p85β, a critical region required for inhibition of p110, as being required for SUMO conjugation. A SUMOylation-defective mutant p85β shows higher activation of the PI3K pathway, and increased cell migration and transformation. Moreover, the cancer-related KS459del mutant in p85α was less efficiently SUMOylated compared with the wild-type protein. Finally, our results show that SUMO modulates p85 tyrosine phosphorylation, a modification correlating with PI3K pathway activation. Thus, SUMO reduces the levels of tyrosine-phosphorylated-p85 while loss of SUMOylation results in increased tyrosine phosphorylation of p85. In summary, we identify SUMO as a new important player in the regulation of the PI3K pathway through modulation of p85.

Indexed as

Amino Acid SequenceAnimalsClass Ia Phosphatidylinositol 3-KinaseHumansMutationPhosphorylationProtein BindingSmall Ubiquitin-Related Modifier ProteinsClass Ia Phosphatidylinositol 3-KinaseSmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID26411363
OpenAlexW2231621831

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.