Evidence map›Paper›PMID 22451918›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Drosophila Mgr, a Prefoldin subunit cooperating with von Hippel Lindau to regulate tubulin stability.

Nathalie Delgehyr, Uta Wieland, Hélène Rangone, Xavier Pinson, Guojie Mao, Nikola S Dzhindzhev, Doris McLean, Maria G Riparbelli, Salud Llamazares, Giuliano Callaini and 2 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

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  18. Microtubules in plants.The arabidopsis book · 2015
    Article
  19. Review
  20. VBP1 facilitates proteasome and autophagy-mediated degradation of MutS homologue hMSH4.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 3 countries.

Nathalie DelgehyrDepartment of Genetics, Cancer Research United Kingdom Cell Cycle Genetics Research Group, University of Cambridge, Cambridge CB2 3EH, United Kingdom.
Uta Wieland
Hélène Rangone
Xavier Pinson
Guojie Mao
Nikola S Dzhindzhev
Doris McLean
Maria G Riparbelli
Salud Llamazares
Giuliano Callaini
Cayetano Gonzalez
David M Glover
Cancer Research UK · GBInstitute for Research in Biomedicine · ESUniversity of Siena · ITUniversity of Cambridge · GB

Funding

Cancer Research UK 11431
6 · The paper itself

Abstract

Mutations in Drosophila merry-go-round (mgr) have been known for over two decades to lead to circular mitotic figures and loss of meiotic spindle integrity. However, the identity of its gene product has remained undiscovered. We now show that mgr encodes the Prefoldin subunit counterpart of human von Hippel Lindau binding-protein 1. Depletion of Mgr from cultured cells also leads to formation of monopolar and abnormal spindles and centrosome loss. These phenotypes are associated with reductions of tubulin levels in both mgr flies and mgr RNAi-treated cultured cells. Moreover, mgr spindle defects can be phenocopied by depleting β-tubulin, suggesting Mgr function is required for tubulin stability. Instability of β-tubulin in the mgr larval brain is less pronounced than in either mgr testes or in cultured cells. However, expression of transgenic β-tubulin in the larval brain leads to increased tubulin instability, indicating that Prefoldin might only be required when tubulins are synthesized at high levels. Mgr interacts with Drosophila von Hippel Lindau protein (Vhl). Both proteins interact with unpolymerized tubulins, suggesting they cooperate in regulating tubulin functions. Accordingly, codepletion of Vhl with Mgr gives partial rescue of tubulin instability, monopolar spindle formation, and loss of centrosomes, leading us to propose a requirement for Vhl to promote degradation of incorrectly folded tubulin in the absence of functional Prefoldin. Thus, Vhl may play a pivotal role: promoting microtubule stabilization when tubulins are correctly folded by Prefoldin and tubulin destruction when they are not.

Indexed as

AnimalsConserved SequenceDrosophila melanogasterDrosophila ProteinsHumansMicrotubulesMolecular ChaperonesMutationProtein BindingProtein StabilityProtein SubunitsProteolysisSpindle ApparatusTubulinVon Hippel-Lindau Tumor Suppressor Proteinbeta 2 tubulin, DrosophilaDrosophila ProteinsMgr protein, DrosophilaMolecular ChaperonesprefoldinProtein SubunitsTubulinVon Hippel-Lindau Tumor Suppressor Protein

Identifiers

PMID22451918
PMCPMC3326472
OpenAlexW2084116746

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.