Evidence map›Paper›PMID 25280637›Full record

ReviewBiochimica et biophysica acta2015

PI(4,5)P₂-binding effector proteins for vesicle exocytosis.

Thomas F J Martin

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
5.9field-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

75 citing papers in PubMed, 130 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. PI(4,5)PBiochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  7. Article
  8. Review
  9. Iron triggersmBio · 2025
    Article
  10. Lipid metabolism in the adrenal gland.Frontiers in endocrinology · 2025
    Review
  11. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. PI(4,5)P2: signaling the plasma membrane.The Biochemical journal · 2022
    Article
  17. Article
  18. Article
  19. Synaptotagmin rings as high-sensitivity regulators of synaptic vesicle docking and fusion.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Article

15 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

1 author at 1 institution in 1 country.

Thomas F J MartinBiochemistry Department, University of Wisconsin, 433 Babcock Drive, Madison, WI 53706, USA. Electronic address: tfmartin@wisc.edu.
University of Wisconsin–Madison · US

Funding

THE MECHANISM OF ACTION OF THYROTROPIN-RELEASING HORMONER01DK025861 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI MARTIN, THOMAS F. J. · 1986 to 2024
$5.6M
CA++ REGULATION OF SECRETION IN NEUROENDOCRINE CELLSR01DK040428 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI MARTIN, THOMAS F. J. · 1988 to 2015
$4.8M
THE MECHANISM OF ACTION OF THYROTROPIN-RELEASING HORMONER37DK025861 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI MARTIN, THOMAS F. J. · 1991 to 2008
$3.3M
Calcium Regulation of Secretion in Neuroendocrine CellsR01GM119158 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARTIN, THOMAS F. J. · 2016 to 2019
$1.3M
NIDDK NIH HHS DK025861NIDDK NIH HHS DK040428NIDDK NIH HHS R01 DK025861NIDDK NIH HHS R01 DK040428NIDDK NIH HHS R37 DK025861NIGMS NIH HHS R01 GM119158
6 · The paper itself

Abstract

PI(4,5)P₂participates directly in priming and possibly in fusion steps of Ca²⁺-triggered vesicle exocytosis. High concentration nanodomains of PI(4,5)P₂reside on the plasma membrane of neuroendocrine cells. A subset of vesicles that co-localize with PI(4,5)P₂ domains appear to undergo preferential exocytosis in stimulated cells. PI(4,5)P₂directly regulates vesicle exocytosis by recruiting and activating PI(4,5)P₂-binding proteins that regulate SNARE protein function including CAPS, Munc13-1/2, synaptotagmin-1, and other C2 domain-containing proteins. These PI(4,5)P₂effector proteins are coincidence detectors that engage in multiple interactions at vesicle exocytic sites. The SNARE protein syntaxin-1 also binds to PI(4,5)P₂, which promotes clustering, but an activating role for PI(4,5)P₂in syntaxin-1 function remains to be fully characterized. Similar principles underlie polarized constitutive vesicle fusion mediated in part by the PI(4,5)P₂-binding subunits of the exocyst complex (Sec3, Exo70). Overall, focal vesicle exocytosis occurs at sites landmarked by PI(4,5)P2, which serves to recruit and/or activate multifunctional PI(4,5)P₂-binding proteins. This article is part of a Special Issue entitled Phosphoinositides.

Indexed as

AnimalsBiological TransportCalciumCalcium-Binding ProteinsExocytosisGene Expression RegulationNerve Tissue ProteinsPhosphatidylinositol 4,5-DiphosphateProtein BindingSignal TransductionSynaptotagmin ISyntaxin 1Transport VesiclesVesicular Transport ProteinsCalciumCalcium-Binding ProteinsNerve Tissue ProteinsPhosphatidylinositol 4,5-DiphosphateSynaptotagmin ISyntaxin 1Vesicular Transport ProteinsCAPS/CADPSMunc13Phosphatidylinositol(4,5)bisphosphateSNARE proteinSynaptotagminVesicle exocytosis

Identifiers

PMID25280637
PMCPMC4380529
OpenAlexW2031412125

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.