Evidence map›Paper›PMID 26149689›Full record

ArticleThe Journal of biological chemistry2015

The Fanconi Anemia DNA Repair Pathway Is Regulated by an Interaction between Ubiquitin and the E2-like Fold Domain of FANCL.

Jennifer A Miles, Mark G Frost, Eilis Carroll, Michelle L Rowe, Mark J Howard, Ateesh Sidhu, Viduth K Chaugule, Arno F Alpi, Helen Walden

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Ubiquitin-conjugating Enzymes in Cancer.International journal of biological sciences · 2026
    Review
  3. Article
  4. Review
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  8. Review
  9. Emerging Roles of Non-proteolytic Ubiquitination in Tumorigenesis.Frontiers in cell and developmental biology · 2022
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. The Role of PALB2 in the DNA Damage Response and Cancer Predisposition.International journal of molecular sciences · 2017
    Review
  16. Article
  17. Cellular response to DNA interstrand crosslinks: the Fanconi anemia pathway.Cellular and molecular life sciences : CMLS · 2016
    Review
  18. The Fanconi anaemia pathway: new players and new functions.Nature reviews. Molecular cell biology · 2016
    Review
  19. Specificity and disease in the ubiquitin system.Biochemical Society transactions · 2016
    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

9 authors at 4 institutions in 1 country.

Jennifer A MilesProtein Structure and Function Laboratory, Lincoln's Inn Fields Laboratories of the London Research Institute, Cancer Research, United Kingdom, 44 Lincoln's Inn Fields, London WC2A 3LY, United Kingdom.
Mark G FrostMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, United Kingdom.
Eilis CarrollMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, United Kingdom; Scottish Institute for Cell Signalling, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, United Kingdom.
Michelle L RoweProtein Science Group, School of Biosciences, University of Kent, Canterbury, Kent CT2 7NZ, United Kingdom.
Mark J HowardProtein Science Group, School of Biosciences, University of Kent, Canterbury, Kent CT2 7NZ, United Kingdom.
Ateesh SidhuProtein Structure and Function Laboratory, Lincoln's Inn Fields Laboratories of the London Research Institute, Cancer Research, United Kingdom, 44 Lincoln's Inn Fields, London WC2A 3LY, United Kingdom.
Viduth K ChauguleMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, United Kingdom.
Arno F AlpiMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, United Kingdom; Scottish Institute for Cell Signalling, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, United Kingdom. Electronic address: A.F.Alpi@dundee.ac.uk.
Helen WaldenProtein Structure and Function Laboratory, Lincoln's Inn Fields Laboratories of the London Research Institute, Cancer Research, United Kingdom, 44 Lincoln's Inn Fields, London WC2A 3LY, United Kingdom; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, United Kingdom. Electronic address: h.walden@dundee.ac.uk.
The Honourable Society of Lincoln's Inn · GBUniversity of Kent · GBMedical Research Council · GBMRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

Cancer Research UK 17739Medical Research Council MC_UU_12016/12
6 · The paper itself

Abstract

The Fanconi Anemia (FA) DNA repair pathway is essential for the recognition and repair of DNA interstrand crosslinks (ICL). Inefficient repair of these ICL can lead to leukemia and bone marrow failure. A critical step in the pathway is the monoubiquitination of FANCD2 by the RING E3 ligase FANCL. FANCL comprises 3 domains, a RING domain that interacts with E2 conjugating enzymes, a central domain required for substrate interaction, and an N-terminal E2-like fold (ELF) domain. The ELF domain is found in all FANCL homologues, yet the function of the domain remains unknown. We report here that the ELF domain of FANCL is required to mediate a non-covalent interaction between FANCL and ubiquitin. The interaction involves the canonical Ile44 patch on ubiquitin, and a functionally conserved patch on FANCL. We show that the interaction is not necessary for the recognition of the core complex, it does not enhance the interaction between FANCL and Ube2T, and is not required for FANCD2 monoubiquitination in vitro. However, we demonstrate that the ELF domain is required to promote efficient DNA damage-induced FANCD2 monoubiquitination in vertebrate cells, suggesting an important function of ubiquitin binding by FANCL in vivo.

Indexed as

DNA RepairAmino Acid SequenceAnimalsBinding SitesDrosophila melanogasterDrosophila ProteinsFanconi AnemiaFanconi Anemia Complementation Group L ProteinFanconi Anemia Complementation Group ProteinsGene Expression RegulationHumansModels, MolecularMolecular Sequence DataProtein BindingProtein FoldingProtein Interaction Domains and MotifsDrosophila ProteinsFANCD2 protein, XenopusFANCL protein, humanFanconi Anemia Complementation Group L ProteinFanconi Anemia Complementation Group ProteinsRecombinant ProteinsUBE2T protein, humanUbiquitinUbiquitin-Conjugating EnzymesXenopus ProteinsDNA repairE3 ubiquitin ligaseisothermal titration calorimetry (ITC)nuclear magnetic resonance (NMR)structureubiquitin

Identifiers

PMID26149689
PMCPMC4543658
OpenAlexW1548728090

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.