Evidence map›Paper›PMID 35182012›Full record

ArticleMolecular oncology2022

FET fusion oncoproteins interact with BRD4 and SWI/SNF chromatin remodelling complex subtypes in sarcoma.

Malin Lindén, Christoffer Vannas, Tobias Österlund, Lisa Andersson, Ayman Osman, Mandy Escobar, Henrik Fagman, Anders Ståhlberg, Pierre Åman

Open access · goldAbstract read
In one paragraph

Article in Molecular oncology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-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

16 citing papers in PubMed, 21 citations in OpenAlex.

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  9. Epigenetic determinants of fusion-driven sarcomas: paradigms and challenges.Frontiers in cell and developmental biology · 2024
    Article
  10. Review
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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

9 authors at 1 institution in 1 country.

Malin LindénDepartment of Laboratory Medicine, Sahlgrenska Academy, Sahlgrenska Center for Cancer Research, Institute of Biomedicine, University of Gothenburg, Sweden.ORCID 0000-0002-9055-2575
Christoffer VannasDepartment of Laboratory Medicine, Sahlgrenska Academy, Sahlgrenska Center for Cancer Research, Institute of Biomedicine, University of Gothenburg, Sweden.
Tobias ÖsterlundDepartment of Laboratory Medicine, Sahlgrenska Academy, Sahlgrenska Center for Cancer Research, Institute of Biomedicine, University of Gothenburg, Sweden.
Lisa AnderssonDepartment of Laboratory Medicine, Sahlgrenska Academy, Sahlgrenska Center for Cancer Research, Institute of Biomedicine, University of Gothenburg, Sweden.
Ayman OsmanDepartment of Laboratory Medicine, Sahlgrenska Academy, Sahlgrenska Center for Cancer Research, Institute of Biomedicine, University of Gothenburg, Sweden.
Mandy EscobarDepartment of Laboratory Medicine, Sahlgrenska Academy, Sahlgrenska Center for Cancer Research, Institute of Biomedicine, University of Gothenburg, Sweden.
Henrik FagmanDepartment of Laboratory Medicine, Sahlgrenska Academy, Sahlgrenska Center for Cancer Research, Institute of Biomedicine, University of Gothenburg, Sweden.
Anders StåhlbergDepartment of Laboratory Medicine, Sahlgrenska Academy, Sahlgrenska Center for Cancer Research, Institute of Biomedicine, University of Gothenburg, Sweden.
Pierre ÅmanDepartment of Laboratory Medicine, Sahlgrenska Academy, Sahlgrenska Center for Cancer Research, Institute of Biomedicine, University of Gothenburg, Sweden.ORCID 0000-0002-1482-8875
Sahlgrenska University Hospital · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FET fusion oncoproteins containing one of the FET (FUS, EWSR1, TAF15) family proteins juxtaposed to alternative transcription-factor partners are characteristic of more than 20 types of sarcoma and leukaemia. FET oncoproteins bind to the SWI/SNF chromatin remodelling complex, which exists in three subtypes: cBAF, PBAF and GBAF/ncBAF. We used comprehensive biochemical analysis to characterize the interactions between FET oncoproteins, SWI/SNF complexes and the transcriptional coactivator BRD4. Here, we report that FET oncoproteins bind all three main SWI/SNF subtypes cBAF, PBAF and GBAF, and that FET oncoproteins interact indirectly with BRD4 via their shared interaction partner SWI/SNF. Furthermore, chromatin immunoprecipitation sequencing and proteomic analysis showed that FET oncoproteins, SWI/SNF components and BRD4 co-localize on chromatin and interact with mediator and RNA Polymerase II. Our results provide a possible molecular mechanism for the FET-fusion-induced oncogenic transcriptional profiles and may lead to novel therapies targeting aberrant SWI/SNF complexes and/or BRD4 in FET-fusion-caused malignancies.

Indexed as

Chromatin Assembly and DisassemblySarcomaBromodomain Containing ProteinsCell Cycle ProteinsChromatinChromosomal Proteins, Non-HistoneHumansNuclear ProteinsOncogene ProteinsOncogene Proteins, FusionProteomicsTranscription FactorsBRD4 protein, humanBromodomain Containing ProteinsCell Cycle ProteinsChromatinChromosomal Proteins, Non-HistoneNuclear ProteinsOncogene ProteinsOncogene Proteins, FusionTranscription FactorsBAFBRD4EWSR1-FLI1FUS-DDIT3SarcomaSWI/SNF

Identifiers

PMID35182012
PMCPMC9251840
OpenAlexW4212875294

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.