Evidence map›Paper›PMID 24556335›Full record

ReviewChemistry and physics of lipids2014

Cellular and molecular interactions of phosphoinositides and peripheral proteins.

Robert V Stahelin, Jordan L Scott, Cary T Frick

Open access · greenAbstract readReview
In one paragraph

Review in Chemistry and physics of lipids, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 107 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. An essentialFrontiers in parasitology · 2023
    Article
  10. Article
  11. Article
  12. The intracellular CaProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Binding of CaStructure (London, England : 1993) · 2021
    Article
  17. Article
  18. Article
  19. YPIBP: A repository for phosphoinositide-binding proteins in yeast.Computational and structural biotechnology journal · 2021
    Article
  20. 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

3 authors at 2 institutions in 1 country.

Robert V StahelinDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine-South Bend, South Bend, IN 46617, United States; Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, United States; Mike and Josie Harper Cancer Research Institute, University of Notre Dame, Notre Dame, IN 46556, United States. Electronic address: rstaheli@iupui.edu.
Jordan L ScottDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, United States; Mike and Josie Harper Cancer Research Institute, University of Notre Dame, Notre Dame, IN 46556, United States.
Cary T FrickDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, United States.
University of Notre Dame · USIndiana University South Bend · US

Funding

Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
LIPID-PROTEIN INTERACTIONS IN VIRAL ASSEMBLY AND VIRUS LIKE PARTICLE FORMATIONR01AI081077 · NIAID · PURDUE UNIVERSITY · PI STAHELIN, ROBERT VIRGIL · 2009 to 2019
$3.5M
NIAID NIH HHS R01 AI081077NIGMS NIH HHS T32 GM075762NIGMS NIH HHS T32GM075762
6 · The paper itself

Abstract

Anionic lipids act as signals for the recruitment of proteins containing cationic clusters to biological membranes. A family of anionic lipids known as the phosphoinositides (PIPs) are low in abundance, yet play a critical role in recruitment of peripheral proteins to the membrane interface. PIPs are mono-, bis-, or trisphosphorylated derivatives of phosphatidylinositol (PI) yielding seven species with different structure and anionic charge. The differential spatial distribution and temporal appearance of PIPs is key to their role in communicating information to target proteins. Selective recognition of PIPs came into play with the discovery that the substrate of protein kinase C termed pleckstrin possessed the first PIP binding region termed the pleckstrin homology (PH) domain. Since the discovery of the PH domain, more than ten PIP binding domains have been identified including PH, ENTH, FYVE, PX, and C2 domains. Representative examples of each of these domains have been thoroughly characterized to understand how they coordinate PIP headgroups in membranes, translocate to specific membrane docking sites in the cell, and function to regulate the activity of their full-length proteins. In addition, a number of novel mechanisms of PIP-mediated membrane association have emerged, such as coincidence detection-specificity for two distinct lipid headgroups. Other PIP-binding domains may also harbor selectivity for a membrane physical property such as charge or membrane curvature. This review summarizes the current understanding of the cellular distribution of PIPs and their molecular interaction with peripheral proteins.

Indexed as

AnimalsCellsHumansPhosphatidylinositolsProtein BindingProteinsProtein Structure, TertiaryPhosphatidylinositolsProteinsC2 domainFYVE domainLipid bindingMembrane bindingPeripheral protein.PH domainPhosphoinsoitidePI(3,4,5)P(3)PI(3)PPI(4,5)P(2)

Identifiers

PMID24556335
PMCPMC4484752
OpenAlexW2010093307

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.