Evidence map›Paper›PMID 23552691›Full record

ArticleMolecular biology of the cell2013

Sumoylation of AMPKβ2 subunit enhances AMP-activated protein kinase activity.

Teresa Rubio, Santiago Vernia, Pascual Sanz

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

26 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. SUMO modifies GβL and mediates mTOR signaling.The Journal of biological chemistry · 2024
    Article
  5. Cardioprotective Strategies After Ischemia-Reperfusion Injury.American journal of cardiovascular drugs : drugs, devices, and other interventions · 2024
    Review
  6. Review
  7. Function and regulation of ubiquitin-like SUMO system in heart.Frontiers in cell and developmental biology · 2023
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. SUMOylation-Mediated Response to Mitochondrial Stress.International journal of molecular sciences · 2020
    Review
  15. Review
  16. Article
  17. Sub-cellular localization specific SUMOylation in the heart.Biochimica et biophysica acta. Molecular basis of disease · 2017
    Review
  18. Article
  19. Flow signaling and atherosclerosis.Cellular and molecular life sciences : CMLS · 2017
    Review
  20. Regulation and function of AMPK in physiology and diseases.Experimental & molecular medicine · 2016
    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

3 authors at 1 institution in 2 countries.

Teresa RubioInstituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas, and Centro de Investigación en Red de Enfermedades Raras, 46010-Valencia, Spain.
Santiago Vernia
Pascual Sanz
Fox Chase Cancer Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AMP-activated protein kinase (AMPK) is a sensor of cellular energy status. It is a heterotrimer composed of a catalytic α and two regulatory subunits (β and γ). AMPK activity is regulated allosterically by AMP and by the phosphorylation of residue Thr-172 within the catalytic domain of the AMPKα subunit by upstream kinases. We present evidence that the AMPKβ2 subunit may be posttranslationally modified by sumoylation. This process is carried out by the E3-small ubiquitin-like modifier (SUMO) ligase protein inhibitor of activated STAT PIASy, which modifies the AMPKβ2 subunit by the attachment of SUMO2 but not SUMO1 moieties. Of interest, AMPKβ1 is not a substrate for this modification. We also demonstrate that sumoylation of AMPKβ2 enhances the activity of the trimeric α2β2γ1 AMPK complex. In addition, our results indicate that sumoylation is antagonist and competes with the ubiquitination of the AMPKβ2 subunit. This adds a new layer of complexity to the regulation of the activity of the AMPK complex, since conditions that promote ubiquitination result in inactivation, whereas those that promote sumoylation result in the activation of the AMPK complex.

Indexed as

Gene Expression RegulationProtein Processing, Post-TranslationalAdenosine MonophosphateAmino Acid SequenceAMP-Activated Protein KinasesBinding SitesCell Line, TumorHEK293 CellsHumansMolecular Sequence DataPhosphorylationProtein BindingProtein MultimerizationProtein SubunitsSignal TransductionSmall Ubiquitin-Related Modifier ProteinsAdenosine MonophosphateAMP-Activated Protein KinasesPRKAB2 protein, humanProtein SubunitsSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, human

Identifiers

PMID23552691
PMCPMC3667731
OpenAlexW2170326918

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.