Evidence map›Paper›PMID 10359611›Full record

ArticleMolecular biology of the cell1999

Vimentin dephosphorylation by protein phosphatase 2A is modulated by the targeting subunit B55.

P Turowski, T Myles, B A Hemmings, A Fernandez, N J Lamb

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

46 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. Circulating Vimentin Over-Expression in Patients with Oral Sub Mucosal Fibrosis and Oral Squamous Cell Carcinoma.Indian journal of otolaryngology and head and neck surgery : official publication of the Association of Otolaryngologists of India · 2022
    Article
  4. Vimentin and cytokeratin: Good alone, bad together.Seminars in cancer biology · 2022
    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 at 2 institutions in 2 countries.

P TurowskiCell Biology Unit, Institut de Genetique Humaine, Centre National de la Recherche Scientifique UPR 1142, F-34396 Montpellier Cedex 5, France.
T Myles
B A Hemmings
A Fernandez
N J Lamb
Institut de Génétique Humaine · FRFriedrich Miescher Institute · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The intermediate filament protein vimentin is a major phosphoprotein in mammalian fibroblasts, and reversible phosphorylation plays a key role in its dynamic rearrangement. Selective inhibition of type 2A but not type 1 protein phosphatases led to hyperphosphorylation and concomitant disassembly of vimentin, characterized by a collapse into bundles around the nucleus. We have analyzed the potential role of one of the major protein phosphatase 2A (PP2A) regulatory subunits, B55, in vimentin dephosphorylation. In mammalian fibroblasts, B55 protein was distributed ubiquitously throughout the cytoplasm with a fraction associated to vimentin. Specific depletion of B55 in living cells by antisense B55 RNA was accompanied by disassembly and increased phosphorylation of vimentin, as when type 2A phosphatases were inhibited using okadaic acid. The presence of B55 was a prerequisite for PP2A to efficiently dephosphorylate vimentin in vitro or to induce filament reassembly in situ. Both biochemical fractionation and immunofluorescence analysis of detergent-extracted cells revealed that fractions of PP2Ac, PR65, and B55 were tightly associated with vimentin. Furthermore, vimentin-associated PP2A catalytic subunit was displaced in B55-depleted cells. Taken together these data show that, in mammalian fibroblasts, the intermediate filament protein vimentin is dephosphorylated by PP2A, an event targeted by B55.

Indexed as

PyransSpiro CompoundsAntifungal AgentsCytoplasmEnzyme InhibitorsFibroblastsHumansIntermediate FilamentsInterphaseOkadaic AcidPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 2Recombinant ProteinsVimentinAntifungal AgentsEnzyme InhibitorsOkadaic AcidPhosphoprotein PhosphatasesProtein Phosphatase 2PyransRecombinant ProteinsSpiro CompoundstautomycinVimentin

Identifiers

PMID10359611
PMCPMC25403
OpenAlexW2098489231

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.