Evidence map›Paper›PMID 26934201›Full record

ReviewThe FEBS journal2016

AMP-activated protein kinase: a cellular energy sensor that comes in 12 flavours.

Fiona A Ross, Carol MacKintosh, D Grahame Hardie

Open access · hybridAbstract readReview
In one paragraph

Review in The FEBS journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 204 papers.

0numbers the graph read from it
0cells of the map it votes in
204citing papers in PubMed
21.1field-weighted citation impact, top 1% 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

204 citing papers in PubMed, 365 citations in OpenAlex.

  1. Review
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  17. Review
  18. The AMPK Pathway: Molecular Rejuvenation of Metabolism and Mitochondria.Annual review of cell and developmental biology · 2025
    Review
  19. Article
  20. Article

144 more citing papers are in PubMed but not listed here.

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 1 country.

Fiona A RossDivision of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Scotland, UK.
Carol MacKintoshDivision of Cell and Developmental Biology, School of Life Sciences, University of Dundee, Scotland, UK.
D Grahame HardieDivision of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Scotland, UK.
University of Dundee · GB

Funding

Cancer Research UK 15101Cancer Research UK C37030/A15101Medical Research Council G0801767Wellcome Trust 097726
6 · The paper itself

Abstract

The AMP-activated protein kinase (AMPK) is a sensor of cellular energy status that is expressed in essentially all eukaryotic cells, suggesting that it arose during early eukaryotic evolution. It occurs universally as heterotrimeric complexes containing catalytic α subunits and regulatory β and γ subunits. Although Drosophila melanogaster contains single genes encoding each subunit, in mammals, each subunit exists as multiple isoforms encoded by distinct genes, giving rise to up to 12 heterotrimeric combinations. The multiple isoforms of each subunit are 2R-ohnologues generated by the two rounds of whole genome duplication that occurred at the evolutionary origin of the vertebrates. Although the differential roles of these isoform combinations remain only partly understood, there are indications that they may have different subcellular locations, different inputs and outputs, and different functions. The multiple isoforms are of particular interest with respect to the roles of AMPK in cancer because the genes encoding some isoforms, such as PRKAA1 and PRKAB2 (encoding α1 and β2), are quite frequently amplified in tumour cells, whereas the genes encoding others, such as PRKAA2 (encoding α2), tend to be mutated, which, in some but not all cases, may result in a loss of function. Thus, although AMPK acts downstream of the tumour suppressor liver kinase B1, and some of its isoform combinations may act as tumour suppressors that restrain the growth and proliferation of tumour cells, other isoform combinations may paradoxically act as oncogenes, perhaps by aiding the survival of tumour cells undergoing environmental stresses such as hypoxia or nutrient deprivation.

Indexed as

AMP-Activated Protein KinasesAnimalsEvolution, MolecularHumansIsoenzymesNeoplasmsOncogene ProteinsProtein SubunitsTumor Suppressor ProteinsAMP-Activated Protein KinasesIsoenzymesOncogene ProteinsProtein SubunitsTumor Suppressor Proteins2R-ohnologueadenine nucleotidesAMP-activated protein kinasecancerenergy homeostasisLKB1oncogenetumour suppressor

Identifiers

PMID26934201
PMCPMC4995730
OpenAlexW2320228393

What OpenQuestion holds

Textmetadata
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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.