Evidence map›Paper›PMID 24574051›Full record

ArticleCytoskeleton (Hoboken, N.J.)2014

Phosphorylation of α-tubulin by protein kinase C stimulates microtubule dynamics in human breast cells.

Shatarupa De, Areti Tsimounis, Xiangyu Chen, Susan A Rotenberg

Abstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Tau, microtubule dynamics, and axonal transport: New paradigms for neurodegenerative disease.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  5. Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021
    Review
  6. FKBP25 Regulates Meiotic Apparatus During Mouse Oocyte Maturation.Frontiers in cell and developmental biology · 2021
    Article
  7. Article
  8. Review
  9. Review
  10. Phosphorylation state of SerCellular signalling · 2018
    Article
  11. Article
  12. Tubulin Post-Translational Modifications and Microtubule Dynamics.International journal of molecular sciences · 2017
    Review
  13. Review
  14. The Effect of SIN1 and Microtubules on Insulin Induced PKC ζ Activation.Medical science monitor : international medical journal of experimental and clinical research · 2017
    Article
  15. Article
  16. Article
  17. 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

4 authors at 3 institutions in 1 country.

Shatarupa DeDepartment of Chemistry and Biochemistry, Queens College, The City University of New York, New York, New York; The Graduate Center, The City University of New York, New York.
Areti Tsimounis
Xiangyu Chen
Susan A Rotenberg
City University of New York · USQueens College, CUNY · USThe Graduate Center, CUNY · US

Funding

Protein Kinase C Substrates in Human Breast CancerR15CA125632 · NCI · QUEENS COLLEGE · PI ROTENBERG, SUSAN A. · 2007 to 2013
$930k
NCI NIH HHS CA125632NCI NIH HHS R15 CA125632
6 · The paper itself

Abstract

Protein kinase C (PKC) engenders motility through phosphorylation of α-tubulin at Ser-165 in nontransformed MCF-10A cells. Live cell imaging explored the impact of PKC-mediated phosphorylation on microtubule (MT) dynamics. MTs fluorescently labeled with GFP-α-tubulin were treated with diacylglycerol (DAG)-lactone (a membrane-permeable PKC activator), or cotransfected with a pseudophosphorylated S165D-α6-tubulin mutant. Each condition increased the dynamicity of MTs by stimulating the rate and duration of the growth phase and decreasing the frequency of catastrophe. In MDA-MB-231 metastatic breast cells where the intrinsic PKC activity is high, these MT growth parameters were also high but could be suppressed by expression of phosphorylation-resistant S165N-α6-tubulin or by treatment with a pan-PKC inhibitor (bis-indoleylmaleimide). Subcellular fractionation and immunofluorescence of MCF-10A cells showed that phosphorylation (via DAG-lactone) or pseudophosphorylation of α6-tubulin increased its partitioning into MTs as compared to controls, and produced longer, more stable MTs. Following expression of the plus-end binding protein GFP-EB1, DAG-lactone accelerated the formation and increased the number of nascent MTs. Expression of S165D-α6-tubulin promoted Rac1 activation and Rac1-dependent cell motility. These findings call attention to PKC-mediated phosphorylation of α-tubulin as a novel mechanism for controlling the dynamics of MTs that result in cell movement.

Indexed as

4-ButyrolactoneBreastCell Line, TransformedCell MovementCell SurvivalEnzyme ActivationFemaleFluorescent Antibody TechniqueGreen Fluorescent ProteinsHumansMicrotubule-Associated ProteinsMicrotubulesModels, BiologicalMutant ProteinsNeoplasm MetastasisPhosphorylation(1-(hydroxymethyl)-4-(4-methyl-3-(methylethyl)pentylidene)-3-oxo-2-oxolanyl)methyl 4-methyl-3-(methylethyl)pentanoate4-ButyrolactoneEB1 microtubule binding proteinsenhanced green fluorescent proteinGreen Fluorescent ProteinsMicrotubule-Associated ProteinsMutant ProteinsPhosphoserineProtein Kinase Crac1 GTP-Binding ProteinRecombinant Fusion ProteinsTubulinValerateslive cell imagingmotilitymutantpartitioningRac1

Identifiers

PMID24574051
PMCPMC4113324
OpenAlexW1713278203

What OpenQuestion holds

Textmetadata
LicenceTDM
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.