Evidence map›Paper›PMID 41606197›Full record

ArticleThe EMBO journal2026

Molecular requirements for PLK1 activation by T-loop phosphorylation.

Arianna Esposito-Verza, Duccio Conti, Paulo D Rodrigues Pedroso, Lina Oberste-Lehn, Carolin Koerner, Sabine Wohlgemuth, Artem Mansurkhodzhaev, Ingrid R Vetter, Marion E Pesenti, Andrea Musacchio

Abstract read
In one paragraph

Article in The EMBO journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

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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

10 authors.

Arianna Esposito-VerzaDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany. arianna.espositoverza@mpi-dortmund.mpg.de.ORCID http://orcid.org/0009-0004-9781-9561
Duccio ContiDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.ORCID http://orcid.org/0000-0003-4009-5940
Paulo D Rodrigues PedrosoDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.
Lina Oberste-LehnDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.ORCID http://orcid.org/0009-0006-2977-4351
Carolin KoernerDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.
Sabine WohlgemuthDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.
Artem MansurkhodzhaevDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.
Ingrid R VetterDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.ORCID http://orcid.org/0000-0002-1722-425X
Marion E PesentiDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.ORCID http://orcid.org/0000-0003-3361-8133
Andrea MusacchioDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany. andrea.musacchio@mpi-dortmund.mpg.de.ORCID http://orcid.org/0000-0003-2362-8784

Funding

Deutsche Forschungsgemeinschaft (DFG) CRC1430EC | ERC | HORIZON EUROPE European Research Council (ERC) SyG 951430European Molecular Biology Organization (EMBO) ALFT439-2019Netzwerke-NRW CANTAR network
6 · The paper itself

Abstract

Activation of PLK1, a master mitotic kinase, requires phosphorylation of its activation segment on Thr210, within a basic consensus sequence for Aurora kinases. Aurora B-dependent phosphorylation of Thr210 has been reported, but other evidence identified a strict requirement for the Aurora A partner Bora for Thr210 phosphorylation. Here, we investigate the elusive mechanistic basis for this requirement. We show that Aurora A:Bora phosphorylates Thr210 of PLK1 in vitro. On the contrary, T210 was not phosphorylated by isolated Aurora A, additional Aurora A:activator complexes, or Aurora B:INCENP, even when used at high kinase/substrate ratios. A transient interaction of Bora and PLK1, identified by structural modeling and probed mutationally, is uniquely required for Thr210 phosphorylation. Dependency on Bora for Thr210 phosphorylation is eliminated after mutating Lys208, in the Aurora consensus, into arginine. This conservative mutation turns PLK1 into a substrate of nearly all tested active Aurora kinases, including Aurora B. Collectively, these results shine a new light on the specificity of the PLK1 activation mechanism.

Indexed as

Cell Cycle ProteinsProtein Serine-Threonine KinasesProto-Oncogene ProteinsAurora Kinase AAurora Kinase BEnzyme ActivationHumansPhosphorylationPolo-Like Kinase 1AURKB protein, humanAurora Kinase AAurora Kinase Bbora protein, humanCell Cycle ProteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsAuroraCell CycleKinasekinetochorePolo-like Kinase

Identifiers

PMID41606197
PMCPMC12953774

What Socratic 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 Socratic graph.