Evidence map›Paper›PMID 26519825›Full record

ArticleDNA repair2015

Versatility in phospho-dependent molecular recognition of the XRCC1 and XRCC4 DNA-damage scaffolds by aprataxin-family FHA domains.

Amy L Cherry, Timothy J Nott, Geoffrey Kelly, Stuart L Rulten, Keith W Caldecott, Stephen J Smerdon

Open access · hybridAbstract read
In one paragraph

Article in DNA repair, 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
1.5field-weighted citation impact, top 17% 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, 27 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Amy L CherryFrancis Crick Institute, Mill Hill Laboratory, The Ridgeway, Mill Hill, London NW7 1AA, UK.
Timothy J NottFrancis Crick Institute, Mill Hill Laboratory, The Ridgeway, Mill Hill, London NW7 1AA, UK.
Geoffrey KellyMRC Genome Damage and Stability Centre, University of Sussex, Brighton BN1 9RQ, UK.
Stuart L RultenMRC Genome Damage and Stability Centre, University of Sussex, Brighton BN1 9RQ, UK.
Keith W CaldecottMRC Genome Damage and Stability Centre, University of Sussex, Brighton BN1 9RQ, UK.
Stephen J SmerdonFrancis Crick Institute, Mill Hill Laboratory, The Ridgeway, Mill Hill, London NW7 1AA, UK. Electronic address: Steve.Smerdon@crick.ac.uk.
The Francis Crick Institute · GBUniversity of Sussex · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F013930/1Cancer Research UK 16771Medical Research Council MC_U117533887Medical Research Council MC_U117584228Medical Research Council MR/J006750/1Medical Research Council U117584228
6 · The paper itself

Abstract

Aprataxin, aprataxin and PNKP-like factor (APLF) and polynucleotide kinase phosphatase (PNKP) are key DNA-repair proteins with diverse functions but which all contain a homologous forkhead-associated (FHA) domain. Their primary binding targets are casein kinase 2-phosphorylated forms of the XRCC1 and XRCC4 scaffold molecules which respectively coordinate single-stranded and double-stranded DNA break repair pathways. Here, we present the high-resolution X-ray structure of a complex of phosphorylated XRCC4 with APLF, the most divergent of the three FHA domain family members. This, combined with NMR and biochemical analysis of aprataxin and APLF binding to singly and multiply-phosphorylated forms of XRCC1 and XRCC4, and comparison with PNKP reveals a pattern of distinct but overlapping binding specificities that are differentially modulated by multi-site phosphorylation. Together, our data illuminate important differences between activities of the three phospho-binding domains, in spite of a close evolutionary relationship between them.

Indexed as

DNA DamageAmino Acid SequenceBinding SitesCasein Kinase IICrystallography, X-RayDNA-(Apurinic or Apyrimidinic Site) LyaseDNA-Binding ProteinsDNA RepairDNA Repair EnzymesHumansMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularNuclear ProteinsPhosphorylationPhosphotransferases (Alcohol Group Acceptor)Poly-ADP-Ribose Binding ProteinsAPLF protein, humanAPTX protein, humanCasein Kinase IIDNA-(Apurinic or Apyrimidinic Site) LyaseDNA-Binding ProteinsDNA Repair EnzymesNuclear ProteinsPhosphotransferases (Alcohol Group Acceptor)PNKP protein, humanPoly-ADP-Ribose Binding ProteinsX-ray Repair Cross Complementing Protein 1XRCC1 protein, humanXRCC4 protein, humanDNA break repairDNA-damage signallingFHA domain

Identifiers

PMID26519825
PMCPMC4655838
OpenAlexW2174506244

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.