Evidence map›Paper›PMID 33834259›Full record

ArticleCellular and molecular life sciences : CMLS2021

SUMOylation modulates the stability and function of PI3K-p110β.

Ahmed El Motiam, Carlos F de la Cruz-Herrera, Santiago Vidal, Rocío Seoane, Maite Baz-Martínez, Yanis H Bouzaher, Emilio Lecona, Mariano Esteban, Manuel S Rodríguez, Anxo Vidal and 2 more

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 23 citations in OpenAlex.

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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

12 authors at 6 institutions in 3 countries.

Ahmed El Motiam *Centro de Investigación en Medicina Molecular (CIMUS), CIMUS, P2L7, Universidade de Santiago de Compostela and Instituto de Investigaciones Sanitarias (IDIS), Avda Barcelona, 15706, Santiago de Compostela, Spain.ORCID http://orcid.org/0000-0003-2855-1368
Carlos F de la Cruz-Herrera *Department of Molecular Genetics, University of Toronto, 1 Kings College Circle, Toronto, M5S 1A8, Canada.ORCID http://orcid.org/0000-0002-7493-5154
Santiago VidalCentro de Investigación en Medicina Molecular (CIMUS), CIMUS, P2L7, Universidade de Santiago de Compostela and Instituto de Investigaciones Sanitarias (IDIS), Avda Barcelona, 15706, Santiago de Compostela, Spain.ORCID http://orcid.org/0000-0002-0105-4583
Rocío SeoaneCentro de Investigación en Medicina Molecular (CIMUS), CIMUS, P2L7, Universidade de Santiago de Compostela and Instituto de Investigaciones Sanitarias (IDIS), Avda Barcelona, 15706, Santiago de Compostela, Spain.ORCID http://orcid.org/0000-0002-7536-8702
Maite Baz-MartínezCentro de Investigación en Medicina Molecular (CIMUS), CIMUS, P2L7, Universidade de Santiago de Compostela and Instituto de Investigaciones Sanitarias (IDIS), Avda Barcelona, 15706, Santiago de Compostela, Spain.ORCID http://orcid.org/0000-0001-9160-7833
Yanis H BouzaherCentro de Investigación en Medicina Molecular (CIMUS), CIMUS, P2L7, Universidade de Santiago de Compostela and Instituto de Investigaciones Sanitarias (IDIS), Avda Barcelona, 15706, Santiago de Compostela, Spain.ORCID http://orcid.org/0000-0002-0956-5417
Emilio LeconaCentro de Biología Molecular Severo Ochoa (CSIC-UAM), Universidad Autónoma de Madrid, Cantoblanco, 28049, Madrid, Spain.ORCID http://orcid.org/0000-0002-1687-2562
Mariano EstebanDepartamento de Biología Molecular y Celular, Centro Nacional de Biotecnología (CNB), CSIC, Darwin 3, 28049, Madrid, Spain.ORCID http://orcid.org/0000-0003-0846-2827
Manuel S RodríguezLaboratoire de Chimie de Coordination LCC-UPR 8241-CNRS, Toulouse, France.ORCID http://orcid.org/0000-0001-5445-4495
Anxo VidalCentro de Investigación en Medicina Molecular (CIMUS), CIMUS, P2L7, Universidade de Santiago de Compostela and Instituto de Investigaciones Sanitarias (IDIS), Avda Barcelona, 15706, Santiago de Compostela, Spain.ORCID http://orcid.org/0000-0002-0866-4202
Manuel ColladoInstituto de Investigación Sanitaria de Santiago de Compostela (IDIS), Complexo Hospitalario Universitario de Santiago de Compostela (CHUS), SERGAS, 15706, Santiago de Compostela, Spain.ORCID http://orcid.org/0000-0002-0330-0880
Carmen RivasCentro de Investigación en Medicina Molecular (CIMUS), CIMUS, P2L7, Universidade de Santiago de Compostela and Instituto de Investigaciones Sanitarias (IDIS), Avda Barcelona, 15706, Santiago de Compostela, Spain. mcarmen.rivas@usc.es.ORCID http://orcid.org/0000-0002-0518-7199
Universidade de Santiago de Compostela · ESCentre National de la Recherche Scientifique · FRCentro de Biología Molecular Severo Ochoa · ESCentro Nacional de Biotecnología · ESInstituto de Investigación Sanitaria de Santiago · ESUniversity of Toronto · CA

Funding

Consellería de Cultura, Educación e Ordenación Universitaria, Xunta de Galicia ED431G 2019/02Consellería de Cultura, Educación e Ordenación Universitaria, Xunta de Galicia ED481A-2018/110Consellería de Cultura, Educación e Ordenación Universitaria, Xunta de Galicia ED481A-2020/160Ministerio de Ciencia, Innovación y Universidades BFU-2017-88880-PMinisterio de Ciencia, Innovación y Universidades RTI2018-095818-B-100
6 · The paper itself

Abstract

Class I PI3K are heterodimers composed of a p85 regulatory subunit and a p110 catalytic subunit involved in multiple cellular functions. Recently, the catalytic subunit p110β has emerged as a class I PI3K isoform playing a major role in tumorigenesis. Understanding its regulation is crucial for the control of the PI3K pathway in p110β-driven cancers. Here we sought to evaluate the putative regulation of p110β by SUMO. Our data show that p110β can be modified by SUMO1 and SUMO2 in vitro, in transfected cells and under completely endogenous conditions, supporting the physiological relevance of p110β SUMOylation. We identify lysine residue 952, located at the activation loop of p110β, as essential for SUMOylation. SUMOylation of p110β stabilizes the protein increasing its activation of AKT which promotes cell growth and oncogenic transformation. Finally, we show that the regulatory subunit p85β counteracts the conjugation of SUMO to p110β. In summary, our data reveal that SUMO is a novel p110β interacting partner with a positive effect on the activation of the PI3K pathway.

Indexed as

SumoylationAnimalsCatalytic DomainClass Ia Phosphatidylinositol 3-KinaseEnzyme ActivationEnzyme StabilityHEK293 CellsHumansMiceNIH 3T3 CellsPC-3 CellsSignal TransductionClass Ia Phosphatidylinositol 3-Kinasep110βp85βStabilitySUMOTransformation

Identifiers

PMID33834259
PMCPMC11073289
OpenAlexW3150028332

What Socratic 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 Socratic graph.