Evidence map›Paper›PMID 34836941›Full record

ArticleNature communications2021

A genetically-encoded crosslinker screen identifies SERBP1 as a PKCε substrate influencing translation and cell division.

Silvia Martini, Khalil Davis, Rupert Faraway, Lisa Elze, Nicola Lockwood, Andrew Jones, Xiao Xie, Neil Q McDonald, David J Mann, Alan Armstrong and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Dynamic Assemblies in Genome Maintenance.Advances in experimental medicine and biology · 2026
    Review
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  6. Article
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  14. Review
  15. Genetically encoded crosslinkers to address protein-protein interactions.Protein science : a publication of the Protein Society · 2023
    Review
  16. Review
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

12 authors at 5 institutions in 3 countries.

Silvia Martini *Protein Phosphorylation Laboratory, The Francis Crick Institute, London, UK.
Khalil Davis *Protein Phosphorylation Laboratory, The Francis Crick Institute, London, UK.
Rupert FarawayRNA Network Laboratory, The Francis Crick Institute, London, UK.
Lisa ElzeDepartment of Human Genetics, Radboud University Medical Center, Nijmegen, The Netherlands.ORCID http://orcid.org/0000-0001-6132-2116
Nicola LockwoodProtein Phosphorylation Laboratory, The Francis Crick Institute, London, UK.
Andrew JonesCell Cycle Laboratory, The Francis Crick Institute, London, UK.
Xiao XieSynthetic and Functional Biomolecules Center, Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Neil Q McDonaldSignalling and Structural Biology Laboratory, The Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0003-0975-6325
David J MannDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK.
Alan ArmstrongDepartment of Chemistry, Imperial College, London, UK.ORCID http://orcid.org/0000-0002-3692-3099
Jernej UleRNA Network Laboratory, The Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0002-2452-4277
Peter J ParkerProtein Phosphorylation Laboratory, The Francis Crick Institute, London, UK. peter.parker@crick.ac.uk.ORCID http://orcid.org/0000-0001-5907-6980
The Francis Crick Institute · GBImperial College London · GBKing's College London · GBPeking University · CNRadboud University Nijmegen · NL

Funding

Cancer Research UKMedical Research CouncilWellcome Trust FC001130
6 · The paper itself

Abstract

The PKCε-regulated genome protective pathway provides transformed cells a failsafe to successfully complete mitosis. Despite the necessary role for Aurora B in this programme, it is unclear whether its requirement is sufficient or if other PKCε cell cycle targets are involved. To address this, we developed a trapping strategy using UV-photocrosslinkable amino acids encoded in the PKCε kinase domain. The validation of the mRNA binding protein SERBP1 as a PKCε substrate revealed a series of mitotic events controlled by the catalytic form of PKCε. PKCε represses protein translation, altering SERBP1 binding to the 40 S ribosomal subunit and promoting the assembly of ribonucleoprotein granules containing SERBP1, termed M-bodies. Independent of Aurora B, SERBP1 is shown to be necessary for chromosome segregation and successful cell division, correlating with M-body formation. This requirement for SERBP1 demonstrates that Aurora B acts in concert with translational regulation in the PKCε-controlled pathway exerting genome protection.

Indexed as

Chromosome SegregationMitosisProtein BiosynthesisAurora Kinase BHEK293 CellsHeLa CellsHumansProtein Kinase C-epsilonRNA-Binding ProteinsAURKB protein, humanAurora Kinase BPRKCE protein, humanProtein Kinase C-epsilonRNA-Binding ProteinsSERBP1 protein, human

Identifiers

PMID34836941
PMCPMC8626422
OpenAlexW3217096627

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.