Evidence map›Paper›PMID 26778126›Full record

ArticleMolecular cell2016

Structure of BRCA1-BRCT/Abraxas Complex Reveals Phosphorylation-Dependent BRCT Dimerization at DNA Damage Sites.

Qian Wu, Atanu Paul, Dan Su, Shahid Mehmood, Tzeh Keong Foo, Takashi Ochi, Emma L Bunting, Bing Xia, Carol V Robinson, Bin Wang and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

47 citing papers in PubMed, 73 citations in OpenAlex.

  1. TheBiomolecular NMR assignments · 2026
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  11. Key molecular DNA damage responses of human cells to radiation.Frontiers in cell and developmental biology · 2024
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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

11 authors at 5 institutions in 2 countries.

Qian WuDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, UK.
Atanu PaulDepartment of Genetics, The University of Texas MD Anderson Cancer Center, 1515 Holcombe Boulevard, Houston, TX 77030, USA; Genes and Development Program, The University of Texas Graduate School of Biomedical Sciences at Houston, 6767 Bertner Avenue, Houston, TX 77030, USA.
Dan SuDepartment of Genetics, The University of Texas MD Anderson Cancer Center, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
Shahid MehmoodDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, OX1 3QZ Oxford, UK.
Tzeh Keong FooDepartment of Radiation Oncology, Robert Wood Johnson Medical School, Rutgers Cancer Institute of New Jersey, 195 Little Albany Street, New Brunswick, NJ 08903, USA.
Takashi OchiDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, UK.
Emma L BuntingDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, UK.
Bing XiaDepartment of Radiation Oncology, Robert Wood Johnson Medical School, Rutgers Cancer Institute of New Jersey, 195 Little Albany Street, New Brunswick, NJ 08903, USA.
Carol V RobinsonDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, OX1 3QZ Oxford, UK.
Bin WangDepartment of Genetics, The University of Texas MD Anderson Cancer Center, 1515 Holcombe Boulevard, Houston, TX 77030, USA; Genes and Development Program, The University of Texas Graduate School of Biomedical Sciences at Houston, 6767 Bertner Avenue, Houston, TX 77030, USA. Electronic address: bwang3@mdanderson.org.
Tom L BlundellDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, UK. Electronic address: tom@cryst.bioc.cam.ac.uk.
University of Cambridge · GBThe University of Texas MD Anderson Cancer Center · USUniversity of Oxford · GBRutgers Cancer Institute of New JerseyRutgers, The State University of New Jersey · US

Funding

Role of PALB2 in the DNA Damage Response and Cancer SuppressionR01CA138804 · NCI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI XIA, BING · 2009 to 2024
$5.5M
The role of a novel BRCA1 associated complex in DNA damage response and tumor supR01CA155025 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI WANG, BIN · 2011 to 2020
$3.4M
Medical Research Council 98101Medical Research Council G1000819NCI NIH HHS CA155025NCI NIH HHS R01 CA138804NCI NIH HHS R01CA138804NCI NIH HHS R01 CA155025Wellcome Trust 093167/Z/10/Z
6 · The paper itself

Abstract

BRCA1 accumulation at DNA damage sites is an important step for its function in the DNA damage response and in DNA repair. BRCA1-BRCT domains bind to proteins containing the phosphorylated serine-proline-x-phenylalanine (pSPxF) motif including Abraxas, Bach1/FancJ, and CtIP. In this study, we demonstrate that ionizing radiation (IR)-induces ATM-dependent phosphorylation of serine 404 (S404) next to the pSPxF motif. Crystal structures of BRCT/Abraxas show that phosphorylation of S404 is important for extensive interactions through the N-terminal sequence outside the pSPxF motif and leads to formation of a stable dimer. Mutation of S404 leads to deficiency in BRCA1 accumulation at DNA damage sites and cellular sensitivity to IR. In addition, two germline mutations of BRCA1 are found to disrupt the dimer interface and dimer formation. Thus, we demonstrate a mechanism involving IR-induced phosphorylation and dimerization of the BRCT/Abraxas complex for regulating Abraxas-mediated recruitment of BRCA1 in response to IR.

Indexed as

DNA DamageAmino Acid SequenceAtaxia Telangiectasia Mutated ProteinsBone NeoplasmsBRCA1 ProteinCarrier ProteinsCell Line, TumorCell NucleusCrystallography, X-RayGerm-Line MutationHumansModels, MolecularMolecular Sequence DataOsteosarcomaPhosphorylationProtein BindingABRAXAS1 protein, humanAtaxia Telangiectasia Mutated ProteinsATM protein, humanBRCA1 ProteinBRCA1 protein, humanCarrier ProteinsSerine

Identifiers

PMID26778126
PMCPMC4747905
OpenAlexW2237290032

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.