Evidence map›Paper›PMID 32412594›Full record

ArticleThe Journal of cell biology2020

Phosphorylation of the microtubule-severing AAA+ enzyme Katanin regulates C. elegans embryo development.

Nicolas Joly, Eva Beaumale, Lucie Van Hove, Lisa Martino, Lionel Pintard

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 31% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
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  11. The Mammalian Family of Katanin Microtubule-Severing Enzymes.Frontiers in cell and developmental biology · 2021
    Review
  12. Article
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.

Nicolas JolyProgramme Equipes Labellisées Ligue contre le Cancer - Team "Cell Cycle and Development," Centre National de la Recherche Scientifique - UMR7592, Institut Jacques Monod/University of Paris, Paris, France.
Eva BeaumaleProgramme Equipes Labellisées Ligue contre le Cancer - Team "Cell Cycle and Development," Centre National de la Recherche Scientifique - UMR7592, Institut Jacques Monod/University of Paris, Paris, France.
Lucie Van HoveProgramme Equipes Labellisées Ligue contre le Cancer - Team "Cell Cycle and Development," Centre National de la Recherche Scientifique - UMR7592, Institut Jacques Monod/University of Paris, Paris, France.
Lisa MartinoProgramme Equipes Labellisées Ligue contre le Cancer - Team "Cell Cycle and Development," Centre National de la Recherche Scientifique - UMR7592, Institut Jacques Monod/University of Paris, Paris, France.
Lionel PintardProgramme Equipes Labellisées Ligue contre le Cancer - Team "Cell Cycle and Development," Centre National de la Recherche Scientifique - UMR7592, Institut Jacques Monod/University of Paris, Paris, France.
Institut Jacques Monod · FR

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Ann E. Rougvie · 2012 to 2026
$7.5M
NIH HHS P40 OD010440
6 · The paper itself

Abstract

The evolutionarily conserved microtubule (MT)-severing AAA-ATPase enzyme Katanin is emerging as a critical regulator of MT dynamics. In Caenorhabditis elegans, Katanin MT-severing activity is essential for meiotic spindle assembly but is toxic for the mitotic spindle. Here we analyzed Katanin dynamics in C. elegans and deciphered the role of Katanin phosphorylation in the regulation of its activity and stability. Katanin is abundant in oocytes, and its levels drop after meiosis, but unexpectedly, a significant fraction is present throughout embryogenesis, where it is dynamically recruited to the centrosomes and chromosomes during mitosis. We show that the minibrain kinase MBK-2, which is activated during meiosis, phosphorylates Katanin at multiple serines. We demonstrate unequivocally that Katanin phosphorylation at a single residue is necessary and sufficient to target Katanin for proteasomal degradation after meiosis, whereas phosphorylation at the other sites only inhibits Katanin ATPase activity stimulated by MTs. Our findings suggest that cycles of phosphorylation and dephosphorylation fine-tune Katanin level and activity to deliver the appropriate MT-severing activity during development.

Indexed as

Adaptor Proteins, Signal TransducingAdenosine TriphosphatasesAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsEmbryonic DevelopmentEmbryo, NonmammalianKataninMeiosisMicrotubulesMitosisOocytesPhosphorylationProtein-Tyrosine KinasesRNA InterferenceAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesCaenorhabditis elegans ProteinsKataninMBK-2 protein, C elegansMEI-1 protein, C elegansMel-26 protein, C elegansProtein-Tyrosine Kinases

Identifiers

PMID32412594
PMCPMC7265321
OpenAlexW3025596815

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.