Evidence map›Paper›PMID 30139519›Full record

ReviewBiochemical and biophysical research communications2018

Regulation of actin assembly by PI(4,5)P2 and other inositol phospholipids: An update on possible mechanisms.

Paul A Janmey, Robert Bucki, Ravi Radhakrishnan

Abstract readReview
In one paragraph

Review in Biochemical and biophysical research communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

63 citing papers in PubMed, 109 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Small Nucleolar RNA fromNon-coding RNA · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Multi-Pathway Study for Oxaliplatin Resistance Reduction.Current issues in molecular biology · 2025
    Review
  9. Article
  10. Review
  11. Iron triggersmBio · 2025
    Article
  12. Review
  13. Emerging oralFrontiers in oral health · 2025
    Article
  14. Article
  15. Article
  16. MARCKS and PI(4,5)PMolecular biology of the cell · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Pharmaceutical agent cetylpyridinium chloride inhibits immune mast cell function by interfering with calcium mobilization.Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association · 2023
    Article

3 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 2 countries.

Paul A JanmeyDepartment of Physiology, University of Pennsylvania, Philadelphia, PA, USA; Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, PA, USA. Electronic address: janmey@mail.med.upenn.edu.
Robert BuckiInstitute for Medicine and Engineering, University of Pennsylvania, Philadelphia, PA, USA; Department of Microbiological and Nanobiomedical Engineering, Medical University of Bialystok, Bialystok, Poland.
Ravi RadhakrishnanDepartment of Bioengineering, University of Pennsylvania, Philadelphia, PA, USA.
University of Pennsylvania · US

Funding

Mechanical control of cell growth and differentiationR01GM083272 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI JANMEY, PAUL A · 2008 to 2011
$2.0M
Spatial control of actin assembly by phosphoinositidesR01GM111942 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI JANMEY, PAUL A · 2015 to 2018
$1.8M
NIGMS NIH HHS R01 GM083272NIGMS NIH HHS R01 GM111942
6 · The paper itself

Abstract

Actin cytoskeleton dynamics depend on a tight regulation of actin filament formation from an intracellular pool of monomers, followed by their linkage to each other or to cell membranes, followed by their depolymerization into a fresh pool of actin monomers. The ubiquitous requirement for continuous actin remodeling that is necessary for many cellular functions is orchestrated in large part by actin binding proteins whose affinity for actin is altered by inositol phospholipids, most prominently PI(4,5)P2 (phosphatidylinositol 4,5-bisphosphate). The kinetics of PI(4,5)P2 synthesis and hydrolysis, its lateral distribution within the lipid bilayer, and coincident detection of PI(4,5)P2 and another signal, all play a role in determining when and where a particular PI(4,5)P2-regulated protein is inactivated or activated to exert its effect on the actin cytoskeleton. This review summarizes a range of models that have been developed to explain how PI(4,5)P2 might function in the complex chemical and structural environment of the cell based on a combination of experiment and computational studies.

Indexed as

Actin CytoskeletonActinsAnimalsCell MembraneCytoskeletal ProteinsEukaryotic CellsEzrinGene Expression RegulationHumansKineticsMicrofilament ProteinsModels, BiologicalMyosinsOsteochondrodysplasiasPhosphatidylinositol 4,5-DiphosphatePhospholipase C betaActinsCytoskeletal ProteinsEzrinMicrofilament ProteinsMyosinsPhosphatidylinositol 4,5-DiphosphatePhospholipase C betaPLCB3 protein, humanTalinActin assemblyActin binding proteinsPI(4,5)P2

Identifiers

PMID30139519
PMCPMC6269227
OpenAlexW2885287769

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.