Evidence map›Paper›PMID 28522851›Full record

ArticleScientific reports2017

Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1).

Rasa Sukackaite, Daniela Cornacchia, Malene Ringkjøbing Jensen, Philippe J Mas, Martin Blackledge, Elin Enervald, Guangyou Duan, Tania Auchynnikava, Maja Köhn, Darren J Hart and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

34 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. iScience · 2024
    Article
  7. Article
  8. Article
  9. Untousling the Role of Tousled-like Kinase 1 in DNA Damage Repair.International journal of molecular sciences · 2023
    Review
  10. Article
  11. Article
  12. Temporal control of late replication and coordination of origin firing by self-stabilizing Rif1-PP1 hubs inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Mammalian DNA Replication Timing.Cold Spring Harbor perspectives in biology · 2021
    Review
  18. Article
  19. Review
  20. 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

11 authors at 7 institutions in 7 countries.

Rasa SukackaiteEuropean Molecular Biology Laboratory, Grenoble Outstation, Grenoble, 6 rue Jules Horowitz, 38042, France.
Daniela CornacchiaEuropean Molecular Biology Laboratory, Monterotondo Outstation, Adriano Buzzati-Traverso Campus, Via Ramarini 32, 00015, Monterotondo, Italy.
Malene Ringkjøbing JensenInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 38044, Grenoble, France.
Philippe J MasEuropean Molecular Biology Laboratory, Grenoble Outstation, Grenoble, 6 rue Jules Horowitz, 38042, France.
Martin BlackledgeInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 38044, Grenoble, France.
Elin EnervaldEuropean Molecular Biology Laboratory, Monterotondo Outstation, Adriano Buzzati-Traverso Campus, Via Ramarini 32, 00015, Monterotondo, Italy.
Guangyou DuanGenome Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117, Heidelberg, Germany.
Tania AuchynnikavaWellcome Trust Center for Cell Biology, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh, EH9 3BF, UK.
Maja KöhnGenome Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117, Heidelberg, Germany.ORCID 0000-0001-8142-3504
Darren J HartEuropean Molecular Biology Laboratory, Grenoble Outstation, Grenoble, 6 rue Jules Horowitz, 38042, France. darren.hart@ibs.fr.ORCID 0000-0002-3502-2002
Sara B C BuonomoEuropean Molecular Biology Laboratory, Monterotondo Outstation, Adriano Buzzati-Traverso Campus, Via Ramarini 32, 00015, Monterotondo, Italy. sara.buonomo@ed.ac.uk.ORCID 0000-0002-0177-2884
Centre National de la Recherche Scientifique · FREuropean Molecular Biology Laboratory · FREuropean Molecular Biology Laboratory · ITMemorial Sloan Kettering Cancer Center · USQilu Normal University · CNUniversity of Freiburg · DEWellcome Centre for Cell Biology · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Rif1 is a conserved protein that plays essential roles in orchestrating DNA replication timing, controlling nuclear architecture, telomere length and DNA repair. However, the relationship between these different roles, as well as the molecular basis of Rif1 function is still unclear. The association of Rif1 with insoluble nuclear lamina has thus far hampered exhaustive characterization of the associated protein complexes. We devised a protocol that overcomes this problem, and were thus able to discover a number of novel Rif1 interactors, involved in chromatin metabolism and phosphorylation. Among them, we focus here on PP1. Data from different systems have suggested that Rif1-PP1 interaction is conserved and has important biological roles. Using mutagenesis, NMR, isothermal calorimetry and surface plasmon resonance we demonstrate that Rif1 is a high-affinity PP1 adaptor, able to out-compete the well-established PP1-inhibitor I2 in vitro. Our conclusions have important implications for understanding Rif1 diverse roles and the relationship between the biological processes controlled by Rif1.

Indexed as

AnimalsBinding SitesCell LineMicePoint MutationProtein BindingProtein Phosphatase 1Telomere-Binding ProteinsProtein Phosphatase 1Rif1 protein, mouseTelomere-Binding Proteins

Identifiers

PMID28522851
PMCPMC5437018
OpenAlexW2612617155

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.