Evidence map›Paper›PMID 29167465›Full record

ArticleNature communications2017

Coupling of Polo kinase activation to nuclear localization by a bifunctional NLS is required during mitotic entry.

David Kachaner, Damien Garrido, Haytham Mehsen, Karine Normandin, Hugo Lavoie, Vincent Archambault

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 46 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

6 authors at 2 institutions in 1 country.

David KachanerInstitute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, QC, Canada, H3C 3J7.
Damien GarridoInstitute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, QC, Canada, H3C 3J7.
Haytham MehsenInstitute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, QC, Canada, H3C 3J7.
Karine NormandinInstitute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, QC, Canada, H3C 3J7.
Hugo LavoieInstitute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, QC, Canada, H3C 3J7.
Vincent ArchambaultInstitute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, QC, Canada, H3C 3J7. vincent.archambault.1@umontreal.ca.
Institute for Research in Immunology and Cancer · CAUniversité de Montréal · CA

Funding

CIHR
6 · The paper itself

Abstract

The Polo kinase is a master regulator of mitosis and cytokinesis conserved from yeasts to humans. Polo is composed of an N-term kinase domain (KD) and a C-term polo-box domain (PBD), which regulates its subcellular localizations. The PBD and KD can interact and inhibit each other, and this reciprocal inhibition is relieved when Polo is phosphorylated at its activation loop. How Polo activation and localization are coupled during mitotic entry is unknown. Here we report that PBD binding to the KD masks a nuclear localization signal (NLS). Activating phosphorylation of the KD leads to exposure of the NLS and entry of Polo into the nucleus before nuclear envelope breakdown. Failures of this mechanism result in misregulation of the Cdk1-activating Cdc25 phosphatase and lead to mitotic and developmental defects in Drosophila. These results uncover spatiotemporal mechanisms linking master regulatory enzymes during mitotic entry.

Indexed as

Active Transport, Cell NucleusAmino Acid SequenceAnimalsAnimals, Genetically Modifiedcdc25 PhosphatasesDrosophila melanogasterDrosophila ProteinsEnzyme ActivationFemaleMaleMitosisModels, BiologicalModels, MolecularNuclear Localization SignalsPhosphorylationProtein Interaction Domains and Motifscdc25 PhosphatasesDrosophila ProteinsNuclear Localization Signalspolo protein, DrosophilaProtein Serine-Threonine KinasesRecombinant Fusion Proteins

Identifiers

PMID29167465
PMCPMC5700101
OpenAlexW2950516725

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.