Evidence map›Paper›PMID 32616651›Full record

ArticleThe Journal of biological chemistry2020

The autophagy protein Ambra1 regulates gene expression by supporting novel transcriptional complexes.

Christina Schoenherr, Adam Byron, Billie Griffith, Alexander Loftus, Jimi C Wills, Alison F Munro, Alex von Kriegsheim, Margaret C Frame

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. 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
1.7field-weighted citation impact, top 15% 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, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. m6A demethylase FTO transcriptionally activated by SP1 improves ischemia reperfusion-triggered acute kidney injury by activating Ambra1/ULK1-mediated autophagy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Autophagy · 2023
    Article
  11. Ambra1 in cancer: implications for clinical oncology.Apoptosis : an international journal on programmed cell death · 2022
    Review
  12. Characterisation of a nucleo-adhesome.Nature communications · 2022
    Article
  13. Article
  14. Review
  15. Review
  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

8 authors at 1 institution in 1 country.

Christina SchoenherrCancer Research UK Edinburgh Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.
Adam ByronCancer Research UK Edinburgh Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.
Billie GriffithCancer Research UK Edinburgh Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.
Alexander LoftusCancer Research UK Edinburgh Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.
Jimi C WillsCancer Research UK Edinburgh Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.
Alison F MunroCancer Research UK Edinburgh Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.
Alex von KriegsheimCancer Research UK Edinburgh Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom.
Margaret C FrameCancer Research UK Edinburgh Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom. Electronic address: m.frame@ed.ac.uk.
Edinburgh Cancer Research · GB

Funding

Cancer Research UK 24837Cancer Research UK C157/A24837
6 · The paper itself

Abstract

Ambra1 is considered an autophagy and trafficking protein with roles in neurogenesis and cancer cell invasion. Here, we report that Ambra1 also localizes to the nucleus of cancer cells, where it has a novel nuclear scaffolding function that controls gene expression. Using biochemical fractionation and proteomics, we found that Ambra1 binds to multiple classes of proteins in the nucleus, including nuclear pore proteins, adaptor proteins such as FAK and Akap8, chromatin-modifying proteins, and transcriptional regulators like Brg1 and Atf2. We identified biologically important genes, such as

Indexed as

Gene Expression RegulationSignal TransductionActivating Transcription Factor 2Active Transport, Cell NucleusAdaptor Proteins, Signal TransducingA Kinase Anchor ProteinsAngiopoietin-1Cell LineChromatinDNA HelicasesFocal Adhesion Kinase 1HumansIntegrin alpha ChainsIntegrin beta ChainsMultiprotein ComplexesNuclear ProteinsActivating Transcription Factor 2Adaptor Proteins, Signal TransducingAKAP8 protein, humanA Kinase Anchor ProteinsAMBRA1 protein, humanAngiopoietin-1ANGPT1 protein, humanATF2 protein, humanChromatinDNA HelicasesFocal Adhesion Kinase 1Integrin alpha ChainsIntegrin beta ChainsITGA8 protein, humanITGB7 protein, humanMultiprotein ComplexesNuclear ProteinsPTK2 protein, humanSMARCA4 protein, humanTGFB2 protein, humanTGFB3 protein, humanTranscription FactorsTransforming Growth Factor beta2Transforming Growth Factor beta3Akap8Ambra1Atf2autophagyCdk9chromatinDNA transcriptionnucleustraffickingtranscription

Identifiers

PMID32616651
PMCPMC7443501
OpenAlexW3040292923

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.