Evidence map›Paper›PMID 34264286›Full record

ArticleThe Biochemical journal2021

PARP7 mono-ADP-ribosylates the agonist conformation of the androgen receptor in the nucleus.

Teddy Kamata, Chun-Song Yang, Bryce M Paschal

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. NADCell reports · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Functional roles of ADP-ribosylation writers, readers and erasers.Frontiers in cell and developmental biology · 2022
    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 1 country.

Teddy KamataDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, VA 22908, U.S.A.
Chun-Song YangDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, VA 22908, U.S.A.
Bryce M PaschalDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, VA 22908, U.S.A.ORCID 0000-0001-8593-0503
University of Virginia · US

Funding

Cancer Research Training Program: From Molecular Mechanisms to Therapeutic StrategiesT32CA009109 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Andrew Carl Dudley, Melanie R Rutkowski · 1985 to 2026
$13.9M
Parp Function in Prostate CancerR01CA214872 · NCI · UNIVERSITY OF VIRGINIA · PI Bryce Paschal · 2017 to 2026
$3.6M
NCI NIH HHS R01 CA214872NCI NIH HHS T32 CA009109
6 · The paper itself

Abstract

We recently described a signal transduction pathway that contributes to androgen receptor (AR) regulation based on site-specific ADP-ribosylation by PARP7, a mono-ADP-ribosyltransferase implicated in several human cancers. ADP-ribosylated AR is recognized by PARP9/DTX3L, a heterodimeric complex that contains an ADP-ribose reader (PARP9) and a ubiquitin E3 ligase (DTX3L). Here, we have characterized the cellular and biochemical requirements for AR ADP-ribosylation by PARP7. We found that the reaction requires nuclear localization of PARP7 and an agonist-induced conformation of AR. PARP7 contains a Cys3His1-type zinc finger (ZF), which also is critical for AR ADP-ribosylation. The Parp7 ZF is required for efficient nuclear import by a nuclear localization signal encoded in PARP7, but rescue experiments indicate the ZF makes a contribution to AR ADP-ribosylation that is separable from the effect on nuclear transport. ZF mutations do not detectably reduce PARP7 catalytic activity and binding to AR, but they do result in the loss of PARP7 enhancement of AR-dependent transcription of the MYBPC1 gene. Our data reveals critical roles for AR conformation and the PARP7 ZF in AR ADP-ribosylation and AR-dependent transcription.

Indexed as

ADP Ribose TransferasesADP-RibosylationAndrogensCarrier ProteinsCatalytic DomainCell NucleusGene ExpressionHEK293 CellsHumansMutationMyosin Binding Protein CNeoplasm ProteinsNucleoside Transport ProteinsPoly(ADP-ribose) PolymerasesProtein BindingProtein ConformationADP Ribose TransferasesAndrogensCarrier ProteinsDTX3L protein, humanMyosin Binding Protein CNeoplasm ProteinsNucleoside Transport ProteinsPARP9 protein, humanPoly(ADP-ribose) PolymerasesReceptors, AndrogenTiPARP protein, humanUbiquitin-Protein LigasesADP-ribosylationandrogen receptormono-ADP-ribosyltransferasePARP7prostate cancerTIPARP

Identifiers

PMID34264286
PMCPMC9482820
OpenAlexW3177546514

What OpenQuestion holds

Textmetadata
LicenceTDM
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.