Evidence map›Paper›PMID 32210435›Full record

ArticlePloS one2020

The nuclear receptor NR4A1 is regulated by SUMO modification to induce autophagic cell death.

Gabriela Zárraga-Granados, Gabriel Muciño-Hernández, María R Sánchez-Carbente, Wendy Villamizar-Gálvez, Ana Peñas-Rincón, Cristian Arredondo, María E Andrés, Christopher Wood, Luis Covarrubias, Susana Castro-Obregón

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Controversy and multiple roles of the solitary nucleus receptor Nur77 in disease and physiology.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Deletion of pleiotrophin impairs glucose tolerance and liver metabolism in pregnant mice: Moonlighting role of glycerol kinase.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  11. Article
  12. Review
  13. SUMO modification in apoptosis.Journal of molecular histology · 2021
    Review
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

10 authors at 3 institutions in 2 countries.

Gabriela Zárraga-GranadosDivisión de Neurociencias, Departamento de Neurodesarrollo y Fisiología, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México.
Gabriel Muciño-HernándezDivisión de Neurociencias, Departamento de Neurodesarrollo y Fisiología, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México.
María R Sánchez-CarbenteBiotechnology Research Center, Universidad Autónoma del Estado de Morelos, Cuernavaca, Morelos, México.
Wendy Villamizar-GálvezDivisión de Neurociencias, Departamento de Neurodesarrollo y Fisiología, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México.
Ana Peñas-RincónDivisión de Neurociencias, Departamento de Neurodesarrollo y Fisiología, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México.
Cristian ArredondoDepartamento de Biología Celular y Molecular, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago, Chile.
María E AndrésDepartamento de Biología Celular y Molecular, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago, Chile.
Christopher WoodLaboratorio Nacional de Microscopía Avanzada, Instituto de Biotecnología, UNAM, Cuernavaca, Mexico.
Luis CovarrubiasDepartamento de Genética del Desarrollo y Fisiología Molecular, Instituto de Biotecnología, UNAM, Cuernavaca, Mexico.
Susana Castro-ObregónDivisión de Neurociencias, Departamento de Neurodesarrollo y Fisiología, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City, México.ORCID 0000-0003-0549-5690
Universidad Nacional Autónoma de México · MXPontificia Universidad Católica de Chile · CLUniversidad Autónoma del Estado de Morelos · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NR4A is a nuclear receptor protein family whose members act as sensors of cellular environment and regulate multiple processes such as metabolism, proliferation, migration, apoptosis, and autophagy. Since the ligand binding domains of these receptors have no cavity for ligand interaction, their function is most likely regulated by protein abundance and post-translational modifications. In particular, NR4A1 is regulated by protein abundance, phosphorylation, and subcellular distribution (nuclear-cytoplasmic translocation), and acts both as a transcription factor and as a regulator of other interacting proteins. SUMOylation is a post-translational modification that can affect protein stability, transcriptional activity, alter protein-protein interactions and modify intracellular localization of target proteins. In the present study we evaluated the role of SUMOylation as a posttranslational modification that can regulate the activity of NR4A1 to induce autophagy-dependent cell death. We focused on a model potentially relevant for neuronal cell death and demonstrated that NR4A1 needs to be SUMOylated to induce autophagic cell death. We observed that a triple mutant in SUMOylation sites has reduced SUMOylation, increased transcriptional activity, altered intracellular distribution, and more importantly, its ability to induce autophagic cell death is impaired.

Indexed as

Autophagic Cell DeathCell NucleusCytoplasmHEK293 CellsHumansNuclear Receptor Subfamily 4, Group A, Member 1Nuclear Receptor Subfamily 4, Group A, Member 2PhosphorylationProtein StabilityReceptors, Neurokinin-1Small Ubiquitin-Related Modifier ProteinsSubstance PSumoylationTranscriptional ActivationTranscription FactorsTransfectionNR4A1 protein, humanNR4A2 protein, humanNuclear Receptor Subfamily 4, Group A, Member 1Nuclear Receptor Subfamily 4, Group A, Member 2Receptors, Neurokinin-1Small Ubiquitin-Related Modifier ProteinsSubstance PTACR1 protein, humanTranscription Factors

Identifiers

PMID32210435
PMCPMC7094859
OpenAlexW3013596941

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.