Evidence map›Paper›PMID 32510829›Full record

ArticleEMBO reports2020

Differential functions of FANCI and FANCD2 ubiquitination stabilize ID2 complex on DNA.

Martin L Rennie, Kimon Lemonidis, Connor Arkinson, Viduth K Chaugule, Mairi Clarke, James Streetley, Laura Spagnolo, Helen Walden

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 44 citations in OpenAlex.

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  20. Structural basis of FANCD2 deubiquitination by USP1-UAF1.Nature structural & molecular biology · 2021
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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

8 authors at 1 institution in 1 country.

Martin L RennieInstitute of Molecular Cell and Systems Biology, College of Medical Veterinary and Life Sciences, University of Glasgow, Glasgow, UK.
Kimon LemonidisInstitute of Molecular Cell and Systems Biology, College of Medical Veterinary and Life Sciences, University of Glasgow, Glasgow, UK.
Connor ArkinsonInstitute of Molecular Cell and Systems Biology, College of Medical Veterinary and Life Sciences, University of Glasgow, Glasgow, UK.
Viduth K ChauguleInstitute of Molecular Cell and Systems Biology, College of Medical Veterinary and Life Sciences, University of Glasgow, Glasgow, UK.
Mairi ClarkeScottish Centre for Macromolecular Imaging, University of Glasgow, Glasgow, UK.
James StreetleyScottish Centre for Macromolecular Imaging, University of Glasgow, Glasgow, UK.ORCID 0000-0001-7808-605X
Laura SpagnoloInstitute of Molecular Cell and Systems Biology, College of Medical Veterinary and Life Sciences, University of Glasgow, Glasgow, UK.
Helen WaldenInstitute of Molecular Cell and Systems Biology, College of Medical Veterinary and Life Sciences, University of Glasgow, Glasgow, UK.ORCID 0000-0002-4289-4810
University of Glasgow · GB

Funding

H2020 European Research Council (ERC) ERC-2015-CoG-681582 ICLUbMedical Research Council MC_PC_17135Medical Research Council MC_UU_12016/12UK Research and Innovation | Medical Research Council (MRC) MC_PC_17135
6 · The paper itself

Abstract

The Fanconi anaemia (FA) pathway is a dedicated pathway for the repair of DNA interstrand crosslinks and is additionally activated in response to other forms of replication stress. A key step in the FA pathway is the monoubiquitination of each of the two subunits (FANCI and FANCD2) of the ID2 complex on specific lysine residues. However, the molecular function of these modifications has been unknown for nearly two decades. Here, we find that ubiquitination of FANCD2 acts to increase ID2's affinity for double-stranded DNA via promoting a large-scale conformational change in the complex. The resulting complex encircles DNA, by forming a secondary "Arm" ID2 interface. Ubiquitination of FANCI, on the other hand, largely protects the ubiquitin on FANCD2 from USP1-UAF1 deubiquitination, with key hydrophobic residues of FANCI's ubiquitin being important for this protection. In effect, both of these post-translational modifications function to stabilize a conformation in which the ID2 complex encircles DNA.

Indexed as

Fanconi AnemiaDNADNA DamageDNA RepairFanconi Anemia Complementation Group D2 ProteinFanconi Anemia Complementation Group ProteinsHumansInhibitor of Differentiation Protein 2UbiquitinationDNAFANCD2 protein, humanFANCI protein, humanFanconi Anemia Complementation Group D2 ProteinFanconi Anemia Complementation Group ProteinsID2 protein, humanInhibitor of Differentiation Protein 2deubiquitinationDNA repairFanconi anaemiaprotein-DNA interactionsubiquitin

Identifiers

PMID32510829
PMCPMC7332966
OpenAlexW3033889308

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.