Evidence map›Paper›PMID 11387220›Full record

ArticleThe EMBO journal2001

Requirement of Hsp90 for centrosomal function reflects its regulation of Polo kinase stability.

G de Cárcer, M do Carmo Avides, M J Lallena, D M Glover, C González

Abstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Over-expression of Hsp83 in grossly depletedJournal of biosciences · 2019
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  11. The therapeutic target Hsp90 and cancer hallmarks.Current pharmaceutical design · 2013
    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.

G de CárcerCell Biology and Biophysics, and Gene Expression Programmes, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
M do Carmo Avides
M J Lallena
D M Glover
C González

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have previously shown that the molecular chaperone heat shock protein 90 (Hsp90) is required to ensure proper centrosome function in Drosophila and vertebrate cells. This observation led to the hypothesis that this chaperone could be required for the stability of one or more centrosomal proteins. We have found that one of these is Polo, a protein kinase known to regulate several aspects of cell division including centrosome maturation and function. Inhibition of Hsp90 results in the inactivation of Polo kinase activity. It also leads to a loss in the ability of cytoplasmic extracts to complement the failure of salt-stripped preparations of centrosomes to nucleate microtubules. This effect can be rescued upon addition of active recombinant POLO: We also show that Polo and Hsp90 are part of a complex and conclude that stabilization of Polo is one of the mechanisms by which Hsp90 contributes to the maintenance of functional centrosomes.

Indexed as

Drosophila ProteinsAnimalsCell DivisionCell LineCentrosomeDrosophila melanogasterEmbryo, NonmammalianGenetic Complementation TestHSP90 Heat-Shock ProteinsProtein Serine-Threonine KinasesRecombinant ProteinsVertebratesDrosophila ProteinsHSP90 Heat-Shock Proteinspolo protein, DrosophilaProtein Serine-Threonine KinasesRecombinant Proteins

Identifiers

PMID11387220
PMCPMC125474

What OpenQuestion holds

Textmetadata
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Registered trials

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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.