Evidence map›Paper›PMID 7667304›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Close association of the alpha subunits of Gq and G11 G proteins with actin filaments in WRK1 cells: relation to G protein-mediated phospholipase C activation.

J Ibarrondo, D Joubert, M N Dufour, A Cohen-Solal, V Homburger, S Jard, G Guillon

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. 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
3.7field-weighted citation impact, top 6% 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, 66 citations in OpenAlex.

  1. Article
  2. Review
  3. Phosphatidylinositol 4,5-bisphosphate modifies tubulin participation in phospholipase Cbeta1 signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
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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

7 authors at 1 institution in 1 country.

J IbarrondoCentre de Pharmacologie Endocrinologie, Institut National de la Santé et de la Recherche Médicale, Montpellier, France.
D Joubert
M N Dufour
A Cohen-Solal
V Homburger
S Jard
G Guillon
Institut National de Santé Publique · TN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A selective polyclonal antibody directed toward the C-terminal decapeptide common to the alpha subunits of Gq and G11 G proteins (G alpha q/G alpha 11) was prepared and used to investigate the subcellular distribution fo these proteins in WRK1 cells, a rat mammary tumor cell line. In immunoblots, the antibody recognized purified G alpha q and G alpha 11 proteins and labeled only two bands corresponding to these alpha subunits. Functional studies indicated that this antibody inhibited vasopressin- and guanosine 5'-[alpha-thio]triphosphate-sensitive phospholipase C activities. Immunofluorescence experiments done with this antibody revealed a filamentous labeling corresponding to intracytoplasmic and perimembranous actin-like filament structures. Colocalization of G alpha q/G alpha 11 and F-actin filaments (F-actin) was demonstrated by double-labeling experiments with anti-G alpha q/G alpha 11 and anti-actin antibodies. Immunoblot analysis of membrane, cytoskeletal, and F-actin-rich fractions confirmed the close association of G alpha q/G alpha 11 with actin. Large amounts of G alpha q/G alpha 11 were recovered in the desmin- and tubulin-free F-actin-rich fraction obtained by a double depolymerization-repolymerization cycle. Disorganization of F-actin filaments with cytochalasin D preserved G alpha q/G alpha 11 and F-actin colocalization but partially inhibited vasopressin- and fluoroaluminate-sensitive phospholipase C activity, suggesting that actin-associated G alpha q/G alpha 11 proteins play a role in signal transduction.

Indexed as

ActinsAluminum CompoundsAnimalsColchicineColforsinCyclic AMPCytochalasin DCytoskeletonEnzyme ActivationFluoridesGTP-Binding ProteinsImmunohistochemistryInositol PhosphatesRatsTumor Cells, CulturedType C PhospholipasesActinsAluminum Compoundsaluminum fluorideColchicineColforsinCyclic AMPCytochalasin DFluoridesGTP-Binding ProteinsInositol PhosphatesType C PhospholipasesVasopressins

Identifiers

PMID7667304
PMCPMC41167
OpenAlexW2051034190

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.