Evidence map›Paper›PMID 8890161›Full record

ArticleThe EMBO journal1996

The conserved mitotic kinase polo is regulated by phosphorylation and has preferred microtubule-associated substrates in Drosophila embryo extracts.

A A Tavares, D M Glover, C E Sunkel

Abstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

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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

33 citing papers in PubMed.

  1. Article
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  8. Dissecting protein interactions during cytokinesis.Communicative & integrative biology · 2011
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  19. Cdc5 interacts with the Wee1 kinase in budding yeast.Molecular and cellular biology · 2001
    Article
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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

3 authors.

A A TavaresCancer Research Campaign Cell Cycle Genetics Group, Department of Anatomy and Physiology, Medical Science Institute, The University of Dundee, UK.
D M Glover
C E Sunkel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Drosophila gene polo encodes a protein kinase required for progression through mitosis. Wild-type polo protein migrates as a tight doublet of 67 kDa which is converted to a single band by phosphatase treatment, which also inactivates the kinase. We have determined putative polo substrates in a cell-free system derived from mutant embryos. Exogenous polo protein kinase phosphorylates proteins of sizes 220 kDa, 85 kDa and 54 kDa, to a greater extent when added to extracts of polo(1)-derived embryos compared with extracts of wild-type embryos, which in both cases have been subject to mild heat treatment to inactivate endogenous kinases. Proteins of the same size are predominantly phosphorylated by the endogenous kinases present in wild-type extracts, and are either not phosphorylated or are poorly phosphorylated in extracts of polo(1)-derived embryos. We show that a specific monoclonal antibody to beta-tubulin precipitates the phosphorylated 54 kDa protein together with an associated 85 kDa protein also phosphorylated by polo protein kinase. Moreover polo binds to an 85 kDa protein which is enriched in microtubule preparations. We discuss the extent to which these in vitro phosphorylation results reflect the effects of mutations in polo on microtubule behaviour during the mitotic cycle.

Indexed as

Drosophila ProteinsGene Expression Regulation, DevelopmentalMitosisAnimalsAntibodies, MonoclonalBlotting, WesternDrosophila melanogasterMicrotubule-Associated ProteinsMolecular WeightPhosphorylationProtein Serine-Threonine KinasesTubulinAntibodies, MonoclonalDrosophila ProteinsMicrotubule-Associated Proteinspolo protein, DrosophilaProtein Serine-Threonine KinasesTubulin

Identifiers

PMID8890161
PMCPMC452225

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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.