Evidence map›Paper›PMID 22374089›Full record

ReviewSub-cellular biochemistry2012

Role of PI(4,5)P(2) in vesicle exocytosis and membrane fusion.

Thomas F J Martin

Abstract 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 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
12.7field-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

50 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. PI(4,5)PBiochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. MARCKS and PI(4,5)PMolecular biology of the cell · 2024
    Article
  11. Review
  12. Article
  13. Review
  14. Non-Vesicular Lipid Transport Machinery inInternational journal of molecular sciences · 2023
    Review
  15. Review
  16. Article
  17. Lipids and Secretory Vesicle Exocytosis.Advances in neurobiology · 2023
    Article
  18. CaAdvances in experimental medicine and biology · 2023
    Article
  19. Article
  20. Article
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 MartinDepartment of Biochemistry, University of Wisconsin-Madison, 433 Babcock Drive, 53706, Madison, WI, U.S.A, 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
NIDDK NIH HHS R01 DK025861NIDDK NIH HHS R01 DK040428
6 · The paper itself

Abstract

A role for phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)) in membrane fusion was originally identified for regulated dense-core vesicle exocytosis in neuroendocrine cells. Subsequent studies demonstrated essential roles for PI(4,5)P(2) in regulated synaptic vesicle and constitutive vesicle exocytosis. For regulated dense-core vesicle exocytosis, PI(4,5)P(2) appears to be primarily required for priming, a stage in vesicle exocytosis that follows vesicle docking and precedes Ca(2) (+)-triggered fusion. The priming step involves the organization of SNARE protein complexes for fusion. A central issue concerns the mechanisms by which PI(4,5)P(2) exerts an essential role in membrane fusion events at the plasma membrane. The observed microdomains of PI(4,5)P(2) in the plasma membrane of neuroendocrine cells at fusion sites has suggested possible direct effects of the phosphoinositide on membrane curvature and tension. More likely, PI(4,5)P(2) functions in vesicle exocytosis as in other cellular processes to recruit and activate PI(4,5)P(2)-binding proteins. CAPS and Munc13 proteins, which bind PI(4,5)P(2) and function in vesicle priming to organize SNARE proteins, are key candidates as effectors for the role of PI(4,5)P(2) in vesicle priming. Consistent with roles prior to fusion that affect SNARE function, subunits of the exocyst tethering complex involved in constitutive vesicle exocytosis also bind PI(4,5)P(2). Additional roles for PI(4,5)P(2) in fusion pore dilation have been described, which may involve other PI(4,5)P(2)-binding proteins such as synaptotagmin. Lastly, the SNARE proteins that mediate exocytic vesicle fusion contain highly basic membrane-proximal domains that interact with acidic phospholipids that likely affect their function.

Indexed as

Membrane FusionAnimalsCalciumCalcium-Binding ProteinsCell MembraneEukaryotic CellsExocytosisHumansPhosphatidylinositol 4,5-DiphosphateQa-SNARE ProteinsSignal TransductionSynaptosomal-Associated Protein 25SynaptotagminsTransport VesiclesVesicle-Associated Membrane Protein 2CalciumCalcium-Binding ProteinsCAPS protein, humanPhosphatidylinositol 4,5-DiphosphateQa-SNARE ProteinsSynaptosomal-Associated Protein 25SynaptotagminsVesicle-Associated Membrane Protein 2

Identifiers

PMID22374089
PMCPMC3978774
OpenAlexW1588803833

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.