Evidence map›Paper›PMID 18832073›Full record

ArticleGenes & development2008

Sequestration of Polo kinase to microtubules by phosphopriming-independent binding to Map205 is relieved by phosphorylation at a CDK site in mitosis.

Vincent Archambault, Pier Paolo D'Avino, Michael J Deery, Kathryn S Lilley, David M Glover

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed, 77 citations in OpenAlex.

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  13. Exo1 recruits Cdc5 polo kinase to MutLγ to ensure efficient meiotic crossover formation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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  16. Coordination of Embryogenesis by the Centrosome in Drosophila melanogaster.Results and problems in cell differentiation · 2019
    Review
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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

5 authors at 1 institution in 1 country.

Vincent ArchambaultDepartment of Genetics, University of Cambridge, Cambridge, CB2 3EH, United Kingdom.
Pier Paolo D'Avino
Michael J Deery
Kathryn S Lilley
David M Glover
University of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research CouncilCancer Research UKMedical Research Council G0501718
6 · The paper itself

Abstract

The conserved Polo kinase controls multiple events in mitosis and cytokinesis. Although Polo-like kinases are regulated by phosphorylation and proteolysis, control of subcellular localization plays a major role in coordinating their mitotic functions. This is achieved largely by the Polo-Box Domain, which binds prephosphorylated targets. However, it remains unclear whether and how Polo might interact with partner proteins when priming mitotic kinases are inactive. Here we show that Polo associates with microtubules in interphase and cytokinesis, through a strong interaction with the microtubule-associated protein Map205. Surprisingly, this interaction does not require priming phosphorylation of Map205, and the Polo-Box Domain of Polo is required but not sufficient for this interaction. Moreover, phosphorylation of Map205 at a CDK site relieves this interaction. Map205 can stabilize Polo and inhibit its cellular activity in vivo. In syncytial embryos, the centrosome defects observed in polo hypomorphs are enhanced by overexpression of Map205 and suppressed by its deletion. We propose that Map205-dependent targeting of Polo to microtubules provides a stable reservoir of Polo that can be rapidly mobilized by the activity of Cdk1 at mitotic entry.

Indexed as

Amino Acid SequenceAnimalsAnimals, Genetically ModifiedBinding SitesCDC2 Protein KinaseCytokinesisDrosophila melanogasterDrosophila ProteinsFemaleInterphaseMicrotubule-Associated ProteinsMicrotubulesMitosisModels, BiologicalMolecular Sequence DataPhosphorylationCDC2 Protein KinaseDrosophila ProteinsMap205 protein, DrosophilaMicrotubule-Associated Proteinspolo protein, DrosophilaProtein Serine-Threonine Kinases

Identifiers

PMID18832073
PMCPMC2559908
OpenAlexW2109796319

What OpenQuestion holds

Textmetadata
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.