Evidence map›Paper›PMID 33799807›Full record

ArticleCells2021

PARP7 and Mono-ADP-Ribosylation Negatively Regulate Estrogen Receptor α Signaling in Human Breast Cancer Cells.

Marit Rasmussen, Susanna Tan, Venkata S Somisetty, David Hutin, Ninni Elise Olafsen, Anders Moen, Jan H Anonsen, Denis M Grant, Jason Matthews

Open access · goldAbstract read
In one paragraph

Article in Cells, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.1field-weighted citation impact, top 4% 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

39 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
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  7. NADCell reports · 2026
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  9. Review
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  13. Rat somatic genome editing enables ER+ breast cancer modeling.bioRxiv : the preprint server for biology · 2025
    Article
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  16. 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 2 institutions in 2 countries.

Marit RasmussenDepartment of Nutrition, Institute of Basic Medical Sciences, Faculty of Medicine, University of Oslo, Sognsvannsveien 9, 0372 Oslo, Norway.
Susanna TanDepartment of Pharmacology and Toxicology, University of Toronto, 1 King's College Circle, Toronto, ON M5S 1A8, Canada.
Venkata S SomisettyDepartment of Nutrition, Institute of Basic Medical Sciences, Faculty of Medicine, University of Oslo, Sognsvannsveien 9, 0372 Oslo, Norway.
David HutinDepartment of Pharmacology and Toxicology, University of Toronto, 1 King's College Circle, Toronto, ON M5S 1A8, Canada.
Ninni Elise OlafsenDepartment of Nutrition, Institute of Basic Medical Sciences, Faculty of Medicine, University of Oslo, Sognsvannsveien 9, 0372 Oslo, Norway.
Anders MoenDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, Blindernveien 31, 0371 Oslo, Norway.
Jan H AnonsenDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, Blindernveien 31, 0371 Oslo, Norway.
Denis M GrantDepartment of Pharmacology and Toxicology, University of Toronto, 1 King's College Circle, Toronto, ON M5S 1A8, Canada.
Jason MatthewsDepartment of Nutrition, Institute of Basic Medical Sciences, Faculty of Medicine, University of Oslo, Sognsvannsveien 9, 0372 Oslo, Norway.ORCID 0000-0002-9815-8636
University of Oslo · NOUniversity of Toronto · CA

Funding

CIHR MOP-125919CIHR MOP-494265Johan Throne Holst Foundation 534611
6 · The paper itself

Abstract

ADP-ribosylation is a post-translational protein modification catalyzed by a family of proteins known as poly-ADP-ribose polymerases. PARP7 (TIPARP; ARTD14) is a mono-ADP-ribosyltransferase involved in several cellular processes, including responses to hypoxia, innate immunity and regulation of nuclear receptors. Since previous studies suggested that PARP7 was regulated by 17β-estradiol, we investigated whether PARP7 regulates estrogen receptor α signaling. We confirmed the 17β-estradiol-dependent increases of PARP7 mRNA and protein levels in MCF-7 cells, and observed recruitment of estrogen receptor α to the promoter of PARP7. Overexpression of PARP7 decreased ligand-dependent estrogen receptor α signaling, while treatment of PARP7 knockout MCF-7 cells with 17β-estradiol resulted in increased expression of and recruitment to estrogen receptor α target genes, in addition to increased proliferation. Co-immunoprecipitation assays revealed that PARP7 mono-ADP-ribosylated estrogen receptor α, and mass spectrometry mapped the modified peptides to the receptor's ligand-independent transactivation domain. Co-immunoprecipitation with truncated estrogen receptor α variants identified that the hinge region of the receptor is required for PARP7-dependent mono-ADP-ribosylation. These results imply that PARP7-mediated mono-ADP-ribosylation may play an important role in estrogen receptor positive breast cancer.

Indexed as

ADP-RibosylationCell ProliferationBreast NeoplasmsEstrogen Receptor alphaEstrogensFemaleGene Expression Regulation, NeoplasticHumansMCF-7 CellsNeoplasm ProteinsNucleoside Transport ProteinsPoly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) PolymerasesSignal TransductionESR1 protein, humanEstrogen Receptor alphaEstrogensGREB1 protein, humanNeoplasm ProteinsNucleoside Transport ProteinsPoly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) PolymerasesTiPARP protein, humanARTD14breast cancerestrogen receptor αmono-ADP-ribosylationPARP7poly ADP-ribose polymeraseTIPARP

Identifiers

PMID33799807
PMCPMC8001409
OpenAlexW3134684911

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.