Evidence map›Paper›PMID 37705456›Full record

ArticleProtein science : a publication of the Protein Society2023

The molecular details of a novel phosphorylation-dependent interaction between MRN and the SOSS complex.

Serene El-Kamand, Mark N Adams, Jacqueline M Matthews, Mar-Dean Du Plessis, Ben Crossett, Angela Connolly, Natasha Breen, Alexander Dudley, Derek J Richard, Roland Gamsjaeger and 1 more

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

4 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. 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

11 authors at 3 institutions in 1 country.

Serene El-KamandSchool of Science, Western Sydney University, Penrith, New South Wales, Australia.
Mark N AdamsCentre for Genomics and Personalised Health, School of Biomedical Sciences, Faculty of Health, Translational Research Institute, Queensland University of Technology, Brisbane, Queensland, Australia.
Jacqueline M MatthewsSchool of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales, Australia.
Mar-Dean Du PlessisSchool of Science, Western Sydney University, Penrith, New South Wales, Australia.
Ben CrossettSydney Mass Spectrometry, University of Sydney, Sydney, New South Wales, Australia.
Angela ConnollySydney Mass Spectrometry, University of Sydney, Sydney, New South Wales, Australia.
Natasha BreenSchool of Science, Western Sydney University, Penrith, New South Wales, Australia.
Alexander DudleySchool of Science, Western Sydney University, Penrith, New South Wales, Australia.
Derek J RichardCentre for Genomics and Personalised Health, School of Biomedical Sciences, Faculty of Health, Translational Research Institute, Queensland University of Technology, Brisbane, Queensland, Australia.
Roland GamsjaegerSchool of Science, Western Sydney University, Penrith, New South Wales, Australia.ORCID 0000-0003-1095-2569
Liza CubedduSchool of Science, Western Sydney University, Penrith, New South Wales, Australia.
The University of Sydney · AUWestern Sydney University · AUTranslational Research Institute · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The repair of double-strand DNA breaks (DSBs) by homologous recombination is crucial in the maintenance of genome integrity. While the key role of the Mre11-Rad50-Nbs1 (MRN) complex in repair is well known, hSSB1 (SOSSB and OBFC2B), one of the main components of the sensor of single-stranded DNA (SOSS) protein complex, has also been shown to rapidly localize to DSB breaks and promote repair. We have previously demonstrated that hSSB1 binds directly to Nbs1, a component of the MRN complex, in a DNA damage-independent manner. However, recruitment of the MRN complex has also been demonstrated by an interaction between Integrator Complex Subunit 3 (INTS3; also known as SOSSA), another member of the SOSS complex, and Nbs1. In this study, we utilize a combined approach of in silico, biochemical, and functional experiments to uncover the molecular details of INTS3 binding to Nbs1. We demonstrate that the forkhead-associated domain of Nbs1 interacts with INTS3 via phosphorylation-dependent binding to INTS3 at Threonine 592, with contributions from Serine 590. Based on these data, we propose a model of MRN recruitment to a DSB via INTS3.

Indexed as

Cell Cycle ProteinsNuclear ProteinsDNA Breaks, Double-StrandedDNA RepairMRE11 Homologue ProteinPhosphorylationCell Cycle ProteinsMRE11 Homologue ProteinNuclear ProteinsDNA repairhSSB1INTS3MRN complexNbs1SOSS complex

Identifiers

PMID37705456
PMCPMC10521234
OpenAlexW4386725778

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.