Evidence map›Paper›PMID 19704162›Full record

ArticleThe Journal of biological chemistry2009

Functional interaction between the Fanconi Anemia D2 protein and proliferating cell nuclear antigen (PCNA) via a conserved putative PCNA interaction motif.

Niall G Howlett, Julie A Harney, Meghan A Rego, Frederick W Kolling, Thomas W Glover

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.1field-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

41 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Revisiting the Function of p21International journal of molecular sciences · 2022
    Review
  6. Inhibition of DNA Repair in Cancer Therapy: Toward a Multi-Target Approach.International journal of molecular sciences · 2020
    Review
  7. sRNA/L1 retrotransposition: using siRNAs and miRNAs to expand the applications of the cell culture-based LINE-1 retrotransposition assay.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. The Fanconi anaemia pathway: new players and new functions.Nature reviews. Molecular cell biology · 2016
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

5 authors at 2 institutions in 1 country.

Niall G HowlettDepartment of Cell and Molecular Biology, University of Rhode Island, Kingston, Rhode Island 02881, USA. nhowlett@mail.uri.edu
Julie A Harney
Meghan A Rego
Frederick W Kolling
Thomas W Glover
University of Rhode Island · USUniversity of Michigan–Ann Arbor · US

Funding

UNDERGRADUATE RESEARCH AND SEMINARSP20RR016457 · NCRR · UNIVERSITY OF RHODE ISLAND · PI SHAKARIAN, ALISON M · 2001 to 2011
$35.5M
ROLE OF FRAGILE SITES IN CHROMOSOME BREAKAGE AND CANCERR01CA043222 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI GLOVER, THOMAS W · 1986 to 2008
$2.5M
NCI NIH HHS R01 CA043222NCI NIH HHS R01CA043222-21NCRR NIH HHS P20 RR016457NCRR NIH HHS P20RR016457-09
6 · The paper itself

Abstract

Fanconi Anemia (FA) is a rare recessive disease characterized by congenital abnormalities, bone marrow failure, and cancer susceptibility. The FA proteins and the familial breast cancer susceptibility gene products, BRCA1 and FANCD1/BRCA2, function cooperatively in the FA-BRCA pathway to repair damaged DNA and to prevent cellular transformation. Activation of this pathway occurs via the mono-ubiquitination of the FANCD2 protein, targeting it to nuclear foci where it co-localizes with FANCD1/BRCA2, RAD51, and PCNA. The regulation of the mono-ubiquitination of FANCD2, as well as its function in DNA repair remain poorly understood. In this study, we have further characterized the interaction between the FANCD2 and PCNA proteins. We have identified a highly conserved, putative FANCD2 PCNA interaction motif (PIP-box), and demonstrate that mutation of this motif disrupts FANCD2-PCNA binding and precludes the mono-ubiquitination of FANCD2. Consequently, the FANCD2 PIP-box mutant protein fails to correct the mitomycin C hypersensitivity of FA-D2 patient cells. Our results suggest that PCNA may function as a molecular platform to facilitate the mono-ubiquitination of FANCD2 and activation of the FA-BRCA pathway.

Indexed as

AnimalsApoptosis Regulatory ProteinsBRCA2 ProteinCell Line, TumorChlorocebus aethiopsCOS CellsDNA DamageDNA RepairFanconi AnemiaFanconi Anemia Complementation Group D2 ProteinHumansMitomycinMutagenesis, Site-DirectedMutationProliferating Cell Nuclear AntigenUbiquitinApoptosis Regulatory ProteinsBLID protein, humanBRCA2 ProteinBRCA2 protein, humanFanconi Anemia Complementation Group D2 ProteinMitomycinProliferating Cell Nuclear AntigenUbiquitin

Identifiers

PMID19704162
PMCPMC2781439
OpenAlexW2012485321

What OpenQuestion holds

Textmetadata
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.