Evidence map›Paper›PMID 36420895›Full record

ArticleNucleic acids research2022

Structural basis for the unique multifaceted interaction of DPPA3 with the UHRF1 PHD finger.

Keiichi Hata, Naohiro Kobayashi, Keita Sugimura, Weihua Qin, Deis Haxholli, Yoshie Chiba, Sae Yoshimi, Gosuke Hayashi, Hiroki Onoda, Takahisa Ikegami and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2022. 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
1.6field-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, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Assessing the functional roles of coevolving PHD finger residues.Protein science : a publication of the Protein Society · 2024
    Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Nondomain biopolymers: Flexible molecular strategies to acquire biological functions.Genes to cells : devoted to molecular & cellular mechanisms · 2023
    Review
  15. Non-histone binding functions of PHD fingers.Trends in biochemical sciences · 2023
    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

16 authors at 5 institutions in 2 countries.

Keiichi HataStructural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29, Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
Naohiro KobayashiRIKEN Center for Biosystems Dynamics Research, Suehiro-cho 1-7-22, Tsurumi, Yokohama, Kanagawa 230-0045, Japan.
Keita SugimuraDivision of Cancer Cell Biology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
Weihua QinFaculty of Biology, Ludwig-Maximilians-Universität München, Munich, Germany.ORCID 0000-0002-4401-4442
Deis HaxholliFaculty of Biology, Ludwig-Maximilians-Universität München, Munich, Germany.
Yoshie ChibaDivision of Cancer Cell Biology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
Sae YoshimiStructural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29, Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
Gosuke HayashiDepartment of Biomolecular Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8603, Japan.
Hiroki OnodaStructural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29, Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.ORCID 0000-0002-5031-4919
Takahisa IkegamiStructural Epigenetics Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29, Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
Christopher B MulhollandFaculty of Biology, Ludwig-Maximilians-Universität München, Munich, Germany.
Atsuya NishiyamaDivision of Cancer Cell Biology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.ORCID 0000-0002-8416-3776
Makoto NakanishiDivision of Cancer Cell Biology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.ORCID 0000-0002-6707-3584
Heinrich LeonhardtFaculty of Biology, Ludwig-Maximilians-Universität München, Munich, Germany.ORCID 0000-0002-5086-6449
Tsuyoshi KonumaStructural Epigenetics Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29, Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
Kyohei AritaStructural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29, Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.ORCID 0000-0002-9762-8405
Yokohama City University · JPLudwig-Maximilians-Universität München · DEThe University of Tokyo · JPNagoya University · JPRIKEN Center for Biosystems Dynamics Research · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin-like with PHD and RING finger domain-containing protein 1 (UHRF1)-dependent DNA methylation is essential for maintaining cell fate during cell proliferation. Developmental pluripotency-associated 3 (DPPA3) is an intrinsically disordered protein that specifically interacts with UHRF1 and promotes passive DNA demethylation by inhibiting UHRF1 chromatin localization. However, the molecular basis of how DPPA3 interacts with and inhibits UHRF1 remains unclear. We aimed to determine the structure of the mouse UHRF1 plant homeodomain (PHD) complexed with DPPA3 using nuclear magnetic resonance. Induced α-helices in DPPA3 upon binding of UHRF1 PHD contribute to stable complex formation with multifaceted interactions, unlike canonical ligand proteins of the PHD domain. Mutations in the binding interface and unfolding of the DPPA3 helical structure inhibited binding to UHRF1 and its chromatin localization. Our results provide structural insights into the mechanism and specificity underlying the inhibition of UHRF1 by DPPA3.

Indexed as

CCAAT-Enhancer-Binding ProteinsPHD Zinc FingersAnimalsChromatinChromosomal Proteins, Non-HistoneDNA MethylationMiceUbiquitin-Protein LigasesCCAAT-Enhancer-Binding ProteinsChromatinChromosomal Proteins, Non-HistoneDppa3 protein, mouseUbiquitin-Protein LigasesUhrf1 protein, mouse

Identifiers

PMID36420895
PMCPMC9757060
OpenAlexW4309908771

What OpenQuestion holds

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LicenceCC BY-NC
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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.