Evidence map›Paper›PMID 22403074›Full record

ReviewSub-cellular biochemistry2012

The phospholipase C isozymes and their regulation.

Aurelie Gresset, John Sondek, T Kendall Harden

Open access · greenAbstract readReview
In one paragraph

Review in Sub-cellular biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed, 1 pooled it
18.3field-weighted citation impact, top 1% 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

93 citing papers in PubMed, 1 synthesis or guideline pooled it, 193 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Inhibitors of Phosphatidylinositol-specific Phospholipase C wit hMedicinal chemistry (Shariqah (United Arab Emirates)) · 2026
    Article
  6. Optogenetic control of PLC-γ1 activity polarizes cell motility.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. An integrated mechanism of GProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. The interaction ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. A molecular mechanism to diversify CaNature communications · 2024
    Article
  17. Article
  18. Review
  19. Review
  20. Article

33 more citing papers are in PubMed but not listed here.

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.

Aurelie GressetDepartment of Pharmacology, University of North Carolina School of Medicine, 27599, Chapel Hill, NC, USA.
John Sondek
T Kendall Harden
University of North Carolina at Chapel Hill · US

Funding

Regulation of Phospholipase CR01GM057391 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SONDEK, JOHN E · 1998 to 2021
$6.9M
NIGMS NIH HHS R01 GM057391
6 · The paper itself

Abstract

The physiological effects of many extracellular neurotransmitters, hormones, growth factors, and other stimuli are mediated by receptor-promoted activation of phospholipase C (PLC) and consequential activation of inositol lipid signaling pathways. These signaling responses include the classically described conversion of phosphatidylinositol(4,5)P(2) to the Ca(2+)-mobilizing second messenger inositol(1,4,5)P(3) and the protein kinase C-activating second messenger diacylglycerol as well as alterations in membrane association or activity of many proteins that harbor phosphoinositide binding domains. The 13 mammalian PLCs elaborate a minimal catalytic core typified by PLC-d to confer multiple modes of regulation of lipase activity. PLC-b isozymes are activated by Gaq- and Gbg-subunits of heterotrimeric G proteins, and activation of PLC-g isozymes occurs through phosphorylation promoted by receptor and non-receptor tyrosine kinases. PLC-e and certain members of the PLC-b and PLC-g subclasses of isozymes are activated by direct binding of small G proteins of the Ras, Rho, and Rac subfamilies of GTPases. Recent high resolution three dimensional structures together with biochemical studies have illustrated that the X/Y linker region of the catalytic core mediates autoinhibition of most if not all PLC isozymes. Activation occurs as a consequence of removal of this autoinhibition.

Indexed as

Gene Expression RegulationSecond Messenger SystemsAnimalsDiglyceridesEnzyme ActivationEukaryotic CellsHeterotrimeric GTP-Binding ProteinsHumansInositol 1,4,5-TrisphosphateIsoenzymesModels, MolecularPhosphatidylinositol 4,5-DiphosphatePhosphorylationProtein Structure, SecondaryProtein Structure, TertiaryType C PhospholipasesDiglyceridesHeterotrimeric GTP-Binding ProteinsInositol 1,4,5-TrisphosphateIsoenzymesPhosphatidylinositol 4,5-DiphosphateType C Phospholipases

Identifiers

PMID22403074
PMCPMC3638883
OpenAlexW199111168

What Socratic 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 Socratic graph.