Evidence map›Paper›PMID 22855535›Full record

ArticleMolecular biology of the cell2012

Novel PKCα-mediated phosphorylation site(s) on cofilin and their potential role in terminating histamine release.

Megumi Sakuma, Yasuhito Shirai, Ken-ichi Yoshino, Maho Kuramasu, Tomofumi Nakamura, Toshihiko Yanagita, Kensaku Mizuno, Izumi Hide, Yoshihiro Nakata, Naoaki Saito

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. 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
0.8field-weighted citation impact, top 28% 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, 24 citations in OpenAlex.

  1. Article
  2. Trop-2, NaOncogene · 2022
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. The role of Pak-interacting exchange factor-β phosphorylation at serines 340 and 583 by PKCγ in dopamine release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  11. Competitive displacement of cofilin can promote actin filament severing.Biochemical and biophysical research communications · 2013
    Article
  12. Functions of cofilin in cell locomotion and invasion.Nature reviews. Molecular cell biology · 2013
    Review
  13. 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

10 authors at 4 institutions in 1 country.

Megumi SakumaLaboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, Kobe, Japan.
Yasuhito Shirai
Ken-ichi Yoshino
Maho Kuramasu
Tomofumi Nakamura
Toshihiko Yanagita
Kensaku Mizuno
Izumi Hide
Yoshihiro Nakata
Naoaki Saito
Kobe University · JPHiroshima University · JPTohoku University · JPUniversity of Miyazaki · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Using specific inhibitors, kinase-negative mutants, and small interfering RNA against protein kinase Cα (PKCα) or PKCβI, we find that PKCβI positively regulates degranulation in rat basophilic leukemia-2H3 cells, whereas PKCα negatively regulates degranulation. Mass spectrometric and mutagenic analyses reveal that PKCα phosphorylates cofilin at Ser-23 and/or Ser-24 during degranulation. Overexpression of a nonphosphorylatable form (S23,24A), but not that of a mutant-mimicking phosphorylated form (S23,24E), increases degranulation. Furthermore, the S23,24A mutant binds to F-actin and retains its depolymerizing and/or cleavage activity; conversely, the S23,24E mutant is unable to sever actin filaments, resulting in F-actin polymerization. In addition, the S23,24E mutant preferentially binds to the 14-3-3ζ protein. Fluorescence-activated cell sorting analysis with fluorescein isothiocyanate-phalloidin and simultaneous observation of degranulation, PKC translocation, and actin polymerization reveals that during degranulation, actin polymerization is dependent on PKCα activity. These results indicate that a novel PKCα-mediated phosphorylation event regulates cofilin by inhibiting its ability to depolymerize F-actin and bind to 14-3-3ζ, thereby promoting F-actin polymerization, which is necessary for cessation of degranulation.

Indexed as

Histamine Release14-3-3 ProteinsActinsAmino Acid SequenceAnimalsBinding SitesCell DegranulationCell Line, TumorCofilin 1Enzyme InhibitorsGreen Fluorescent ProteinsImmunoblottingIndolesMaleimidesMicroscopy, ConfocalMolecular Sequence Data14-3-3 ProteinsActinsCfl1 protein, ratCofilin 1Enzyme InhibitorsGreen Fluorescent ProteinsIndolesMaleimidesProtein Kinase C-alpharuboxistaurinSerine

Identifiers

PMID22855535
PMCPMC3442417
OpenAlexW2158052587

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.