Evidence map›Paper›PMID 11179426›Full record

ArticleMolecular biology of the cell2001

Stathmin/Op18 phosphorylation is regulated by microtubule assembly.

T Küntziger, O Gavet, V Manceau, A Sobel, M Bornens

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Microtubules: Evolving roles and critical cellular interactions.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  4. Article
  5. Article
  6. Article
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  11. Review
  12. Article
  13. Aurora B is required for mitotic chromatin-induced phosphorylation of Op18/Stathmin.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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 2 institutions in 1 country.

T KüntzigerInstitut Curie, Section Recherche, Unité Mixte de Recherche 144 Centre National de la Recherche Scientifique, 75248 Paris Cedex 05, France.
O Gavet
V Manceau
A Sobel
M Bornens
Inserm · FRInstitut Curie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Stathmin/Op 18 is a microtubule (MT) dynamics-regulating protein that has been shown to have both catastrophe-promoting and tubulin-sequestering activities. The level of stathmin/Op18 phosphorylation was proved both in vitro and in vivo to be important in modulating its MT-destabilizing activity. To understand the in vivo regulation of stathmin/Op18 activity, we investigated whether MT assembly itself could control phosphorylation of stathmin/Op18 and thus its MT-destabilizing activity. We found that MT nucleation by centrosomes from Xenopus sperm or somatic cells and MT assembly promoted by dimethyl sulfoxide or paclitaxel induced stathmin/Op18 hyperphosphorylation in Xenopus egg extracts, leading to new stathmin/Op18 isoforms phosphorylated on Ser 16. The MT-dependent phosphorylation of stathmin/Op18 took place in interphase extracts as well, and was also observed in somatic cells. We show that the MT-dependent phosphorylation of stathmin/Op18 on Ser 16 is mediated by an activity associated to the MTs, and that it is responsible for the stathmin/Op18 hyperphosphorylation reported to be induced by the addition of "mitotic chromatin." Our results suggest the existence of a positive feedback loop, which could represent a novel mechanism contributing to MT network control.

Indexed as

Microtubule ProteinsAnimalsCell NucleusCentrosomeEnzyme InhibitorsFemaleHeLa CellsHumansInterphaseMaleMicrotubulesNocodazoleOvumPaclitaxelPhosphoproteinsPhosphorylationEnzyme InhibitorsMicrotubule ProteinsNocodazolePaclitaxelPhosphoproteinsProtein IsoformsSerineStathminSTMN1 protein, humanSTMN1 protein, XenopusXenopus Proteins

Identifiers

PMID11179426
PMCPMC30954
OpenAlexW2041884525

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.