Evidence map›Paper›PMID 21338571›Full record

ArticleArchives of biochemistry and biophysics2011

Protein kinase C phosphorylation of PLCβ1 regulates its cellular localization.

Omozuanvbo Aisiku, Louisa Dowal, Suzanne Scarlata

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Claudin 14/15 play important roles in early wallerian degeneration after rat sciatic nerve injury.Chinese journal of traumatology = Zhonghua chuang shang za zhi · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Role of phospholipase C-β in RNA interference.Advances in biological regulation · 2013
    Review
  12. Article
  13. Article
  14. Review
  15. 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 AisikuDepartment of Physiology and Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA.
Louisa Dowal
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 GM053132NIGMS NIH HHS R01 GM053132
6 · The paper itself

Abstract

Activation of phospholipase Cβ (PLCβ) by G proteins leads to a chain of events that result in an increase in intracellular calcium and activation of protein kinase C (PKC). It has been found that PKC phosphorylates PLCβ1 on S887 in vitro without affecting its enzymatic activity or its ability to be activated by Gα(q) proteins. To understand whether S887 phosphorylation affects the enzyme's activity in cells, we constructed two mutants that mimic the wild type and PKC-phosphorylated enzymes (S887A and S887D). We find that these constructs bind similarly to Gα(q) in vitro. When expressed in HEK293 cells, both mutants associate identically to Gα(q) in both the basal and stimulated states. Both mutants diffuse with similar rates and also interact identically with another known binding partner, translin-associated factor X (TRAX), which associates with PLCβ1 in the cytosol and nucleus. However, the two mutants localize differently in the cell. We find that S887A has a much higher nuclear localization than its S887D counterpart both in HEK293 cells and PC12 cells. Our studies suggest that PKC phosphorylation regulates the level of PLCβ1 cytosolic and nuclear activity by regulating its cellular compartmentalization.

Indexed as

AnimalsCell NucleusDNA-Binding ProteinsHEK293 CellsHumansModels, MolecularPC12 CellsPhospholipase C betaPhosphorylationPoint MutationProtein Kinase CRatsDNA-Binding ProteinsPhospholipase C betaProtein Kinase CTSNAX protein, human

Identifiers

PMID21338571
PMCPMC3081424
OpenAlexW2022187555

What OpenQuestion holds

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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.