Evidence map›Paper›PMID 23775692›Full record

ReviewAdvances in experimental medicine and biology2013

PtdIns(4,5)P2-mediated cell signaling: emerging principles and PTEN as a paradigm for regulatory mechanism.

Arne Gericke, Nicholas R Leslie, Mathias Lösche, Alonzo H Ross

Open access · greenAbstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
11.6field-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

29 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. The potassium channel KNature communications · 2025
    Article
  4. Article
  5. Mechanism of the Regulation of Plasma Cholesterol Levels by PI(4,5)PAdvances in experimental medicine and biology · 2023
    Article
  6. Article
  7. Generating a new mouse model for nuclear PTEN deficiency by a single K13R mutation.Genes to cells : devoted to molecular & cellular mechanisms · 2021
    Article
  8. Article
  9. Binding of CaStructure (London, England : 1993) · 2021
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Defective phosphoinositide metabolism in autism.Journal of neuroscience research · 2017
    Review
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

4 authors at 4 institutions in 2 countries.

Arne GerickeDepartment of Chemistry and Biochemistry, Worcester Polytechnic Institute, Worcester, MA 01609, USA.
Nicholas R Leslie
Mathias Lösche
Alonzo H Ross
Carnegie Mellon University · USUniversity of Dundee · GBUniversity of Massachusetts Chan Medical School · USWorcester Polytechnic Institute · US

Funding

Newly Identified Regulator of Neuronal DifferentiationR01NS021716 · NINDS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI ROSS, ALONZO H · 1985 to 2014
$5.2M
STRUCTURAL&FUNCTIONAL INESTIGATIONS OF AB OLIGOMER INTERACTION/SYNTHETIC MEMBRANEP01AG032131 · NIA · CARNEGIE-MELLON UNIVERSITY · PI DESEMO, MARKUS · 2009 to 2011
$1.9M
Membrane Coupling and Dynamic Reorganization of Gag in Viral BuddingR01GM101647 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI LOESCHE, MATHIAS · 2012 to 2015
$1.2M
Medical Research Council G0801865NIA NIH HHS P01 AG032131NIGMS NIH HHS R01 GM101647NINDS NIH HHS R01 NS021716
6 · The paper itself

Abstract

PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) is a relatively common anionic lipid that regulates cellular functions by multiple mechanisms. Hydrolysis of PtdIns(4,5)P2 by phospholipase C yields inositol trisphosphate and diacylglycerol. Phosphorylation by phosphoinositide 3-kinase yields PtdIns(3,4,5)P3, which is a potent signal for survival and proliferation. Also, PtdIns(4,5)P2 can bind directly to integral and peripheral membrane proteins. As an example of regulation by PtdIns(4,5)P2, we discuss phosphatase and tensin homologue deleted on chromosome 10 (PTEN) in detail. PTEN is an important tumor suppressor and hydrolyzes PtdIns(3,4,5)P3. PtdIns(4,5)P2 enhances PTEN association with the plasma membrane and activates its phosphatase activity. This is a critical regulatory mechanism, but a detailed description of this process from a structural point of view is lacking. The disordered lipid bilayer environment hinders structural determinations of membrane-bound PTEN. A new method to analyze membrane-bound protein measures neutron reflectivity for proteins bound to tethered phospholipid membranes. These methods allow determination of the orientation and shape of membrane-bound proteins. In combination with molecular dynamics simulations, these studies will provide crucial structural information that can serve as a foundation for our understanding of PTEN regulation in normal and pathological processes.

Indexed as

AnimalsCell ProliferationCell SurvivalHumansMembrane ProteinsMolecular Dynamics SimulationPhosphatidylinositol 4,5-DiphosphatePTEN PhosphohydrolaseSignal TransductionMembrane ProteinsPhosphatidylinositol 4,5-DiphosphatePTEN Phosphohydrolase

Identifiers

PMID23775692
PMCPMC3763917
OpenAlexW2071716012

What OpenQuestion 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 OpenQuestion graph.