Evidence map›Paper›PMID 32987353›Full record

ArticleDNA repair2020

Biochemical analysis of TOPBP1 oligomerization.

Ahhyun Kim, Katrina Montales, Kenna Ruis, Holly Senebandith, Hovik Gasparyan, Quinn Cowan, W Matthew Michael

Open access · greenAbstract read
In one paragraph

Article in DNA repair, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

17 citing papers in PubMed, 20 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

7 authors at 1 institution in 1 country.

Ahhyun KimMolecular and Computational Biology Section, Department of Biological Sciences, University of Southern California, Los Angeles, CA, 90089, United States.
Katrina MontalesMolecular and Computational Biology Section, Department of Biological Sciences, University of Southern California, Los Angeles, CA, 90089, United States.
Kenna RuisMolecular and Computational Biology Section, Department of Biological Sciences, University of Southern California, Los Angeles, CA, 90089, United States.
Holly SenebandithMolecular and Computational Biology Section, Department of Biological Sciences, University of Southern California, Los Angeles, CA, 90089, United States.
Hovik GasparyanMolecular and Computational Biology Section, Department of Biological Sciences, University of Southern California, Los Angeles, CA, 90089, United States.
Quinn CowanMolecular and Computational Biology Section, Department of Biological Sciences, University of Southern California, Los Angeles, CA, 90089, United States.
W Matthew MichaelMolecular and Computational Biology Section, Department of Biological Sciences, University of Southern California, Los Angeles, CA, 90089, United States. Electronic address: mattm@usc.edu.
University of Southern California · US

Funding

Mechanistic analysis of ATR signalingR01GM122887 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI MICHAEL, MATTHEW · 2017 to 2020
$1.3M
NIGMS NIH HHS R01 GM122887
6 · The paper itself

Abstract

TOPBP1 is an important scaffold protein that helps orchestrate the cellular response to DNA damage. Although it has been previously appreciated that TOPBP1 can form oligomers, how this occurs and the functional consequences for oligomerization were not yet known. Here, we use protein binding assays and other biochemical techniques to study how TOPBP1 self associates. TOPBP1 contains 9 copies of the BRCT domain, and we report that a subset of these BRCT domains interact with one another to drive oligomerization. An intact BRCT 2 domain is required for TOPBP1 oligomerization and we find that the BRCT1&2 region of TOPBP1 interacts with itself and with the BRCT4&5 pair. RAD9 and RHINO are two heterologous binding partners for TOPBP1's BRCT 1&2 domains, and we show that binding of these partners does not come at the expense of TOPBP1 oligomerization. Furthermore, we show that a TOPBP1 oligomer can simultaneously interact with both RAD9 and RHINO. Lastly, we find that the oligomeric state necessary for TOPBP1 to activate the ATR protein kinase is likely to be a tetramer.

Indexed as

DNA DamageProtein Interaction Domains and MotifsProtein MultimerizationAnimalsAtaxia Telangiectasia Mutated ProteinsCell Cycle ProteinsDNA-Binding ProteinsSignal TransductionXenopusAtaxia Telangiectasia Mutated ProteinsAtr protein, XenopusCell Cycle ProteinsDNA-Binding Proteinsrad9 proteinTopBP1 protein, XenopusATRBRCTCheckpointDNA damageScaffold

Identifiers

PMID32987353
PMCPMC7670859
OpenAlexW3088376645

What OpenQuestion holds

Textmetadata
LicenceTDM
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.