Evidence map›Paper›PMID 15611334›Full record

ArticleThe Journal of cell biology2004

Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles.

Rutilio A Fratti, Youngsoo Jun, Alexey J Merz, Nathan Margolis, William Wickner

Abstract read
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
–field-weighted citation impact
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

115 citing papers in PubMed.

  1. The Interplay of Lipids and Peptides in Membrane Merger.Advances in experimental medicine and biology · 2026
    Review
  2. Article
  3. Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. PI3P regulates multiple stages of membrane fusion.Molecular biology of the cell · 2023
    Article
  16. Frontiers in cellular and infection microbiology · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Phosphatidylinositol 3,5-bisphosphate regulates CaTraffic (Copenhagen, Denmark) · 2020
    Article

55 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

5 authors.

Rutilio A FrattiDepartment of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
Youngsoo Jun
Alexey J Merz
Nathan Margolis
William Wickner

Funding

AUTOIMMUNITY &CONNECTIVE TISSUE BIOLOGY TRAININGT32AR007576 · NIAMS · DARTMOUTH COLLEGE · PI RIGBY, WILLIAM FREDERICK CARSON · 1994 to 2008
$1.7M
NIAMS NIH HHS AR07576-09NIAMS NIH HHS T32 AR007576
6 · The paper itself

Abstract

Membrane microdomains are assembled by lipid partitioning (e.g., rafts) or by protein-protein interactions (e.g., coated vesicles). During docking, yeast vacuoles assemble "vertex" ring-shaped microdomains around the periphery of their apposed membranes. Vertices are selectively enriched in the Rab GTPase Ypt7p, the homotypic fusion and vacuole protein sorting complex (HOPS)-VpsC Rab effector complex, SNAREs, and actin. Membrane fusion initiates at vertex microdomains. We now find that the "regulatory lipids" ergosterol, diacylglycerol and 3- and 4-phosphoinositides accumulate at vertices in a mutually interdependent manner. Regulatory lipids are also required for the vertex enrichment of SNAREs, Ypt7p, and HOPS. Conversely, SNAREs and actin regulate phosphatidylinositol 3-phosphate vertex enrichment. Though the PX domain of the SNARE Vam7p has direct affinity for only 3-phosphoinositides, all the regulatory lipids which are needed for vertex assembly affect Vam7p association with vacuoles. Thus, the assembly of the vacuole vertex ring microdomain arises from interdependent lipid and protein partitioning and binding rather than either lipid partitioning or protein interactions alone.

Indexed as

Intracellular MembranesMembrane FusionMembrane LipidsMembrane ProteinsProtein Transportrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesMembrane LipidsMembrane Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsYPT7 protein, S cerevisiae

Identifiers

PMID15611334
PMCPMC2172599

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.