Evidence map›Paper›PMID 21124736›Full record

ArticlePloS one2010

Identification of a novel binding partner of phospholipase cβ1: translin-associated factor X.

Omozuanvbo R Aisiku, Loren W Runnels, Suzanne Scarlata

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

33 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Impacts of Globo H Ceramide on Tumor Microenvironment.Advances in experimental medicine and biology · 2026
    Review
  3. RNAi Regulator C3PO Promotes Arbovirus Infection in Insect Vectors.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Article
  5. Adenosine AJournal of the American Heart Association · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Deletion of the microRNA-degrading nuclease, translin/trax, prevents pathogenic vascular stiffness.American journal of physiology. Heart and circulatory physiology · 2019
    Article
  13. Article
  14. Review
  15. Review
  16. Phospholipase Cβ1 regulates proliferation of neuronal cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  17. Review
  18. Regulation of the activity of the promoter of RNA-induced silencing, C3PO.Protein science : a publication of the Protein Society · 2017
    Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Omozuanvbo R AisikuDepartment of Physiology and Biophysics, Stony Brook University, Stony Brook, New York, USA.
Loren W Runnels
Suzanne Scarlata
Stony Brook University · US

Funding

ACTIVATION OF PHOSPHOLIPASE C BETA BY G PROTEINSR01GM053132 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI SCARLATA, SUZANNE F · 1995 to 2014
$3.5M
NIGMS NIH HHS R01 GM053132PHS HHS 053132
6 · The paper itself

Abstract

Mammalian phospholipase Cβ1 (PLCβ1) is activated by the ubiquitous Gα(q) family of G proteins on the surface of the inner leaflet of plasma membrane where it catalyzes the hydrolysis of phosphatidylinositol 4,5 bisphosphate. In general, PLCβ1 is mainly localized on the cytosolic plasma membrane surface, although a substantial fraction is also found in the cytosol and, under some conditions, in the nucleus. The factors that localize PLCβ1in these other compartments are unknown. Here, we identified a novel binding partner, translin-associated factor X (TRAX). TRAX is a cytosolic protein that can transit into the nucleus. In purified form, PLCβ1 binds strongly to TRAX with an affinity that is only ten-fold weaker than its affinity for its functional partner, Gα(q). In solution, TRAX has little effect on the membrane association or the catalytic activity of PLCβ1. However, TRAX directly competes with Gα(q) for PLCβ1 binding, and excess TRAX reverses Gα(q) activation of PLCβ1. In C6 glia cells, endogenous PLCβ1 and TRAX colocalize in the cytosol and the nucleus, but not on the plasma membrane where TRAX is absent. In Neuro2A cells expressing enhanced yellow and cyano fluorescent proteins (i.e., eYFP- PLCβ1 and eCFP-TRAX), Förster resonance energy transfer (FRET) is observed mostly in the cytosol and a small amount is seen in the nucleus. FRET does not occur at the plasma membrane where TRAX is not found. Our studies show that TRAX, localized in the cytosol and nucleus, competes with plasma-membrane bound Gα(q) for PLCβ1 binding thus stabilizing PLCβ1 in other cellular compartments.

Indexed as

AnimalsBinding, CompetitiveCell LineCell Line, TumorCell MembraneCell NucleusCytosolDNA-Binding ProteinsFluorescence Resonance Energy TransferGTP-Binding Protein alpha Subunits, Gq-G11Luminescent ProteinsMicroscopy, ConfocalPhospholipase C betaProtein BindingRatsRecombinant Fusion ProteinsDNA-Binding ProteinsGTP-Binding Protein alpha Subunits, Gq-G11Luminescent ProteinsPhospholipase C betaRecombinant Fusion ProteinsTsnax protein, rat

Identifiers

PMID21124736
PMCPMC2993962
OpenAlexW2109694440

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.