Evidence map›Paper›PMID 12566429›Full record

ArticleThe Journal of cell biology2003

Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion.

Li Wang, Alexey J Merz, Kevin M Collins, William Wickner

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

79 citing papers in PubMed, 138 citations in OpenAlex.

  1. Article
  2. Assays of Platelet SNARE-actin Interactions.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. PI3P regulates multiple stages of membrane fusion.Molecular biology of the cell · 2023
    Article
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  9. Review
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19 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

4 authors at 1 institution in 1 country.

Li WangDepartment of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
Alexey J Merz
Kevin M Collins
William Wickner
Dartmouth College · US

Funding

Molecular and Cellular Biology at DartmouthT32GM008704 · NIGMS · DARTMOUTH COLLEGE · PI COMPTON, DUANE A. · 1998 to 2018
$6.8M
NIGMS NIH HHS T32 GM008704NIGMS NIH HHS T32GM08704
6 · The paper itself

Abstract

Vacuole tethering, docking, and fusion proteins assemble into a "vertex ring" around the apposed membranes of tethered vacuoles before catalyzing fusion. Inhibitors of the fusion reaction selectively interrupt protein assembly into the vertex ring, establishing a causal assembly hierarchy: (a) The Rab GTPase Ypt7p mediates vacuole tethering and forms the initial vertex ring, independent of t-SNAREs or actin; (b) F-actin disassembly and GTP-bound Ypt7p direct the localization of other fusion factors; (c) The t-SNAREs Vam3p and Vam7p regulate each other's vertex enrichment, but do not affect Ypt7p localization. The v-SNARE Vti1p is enriched at vertices by a distinct pathway that is independent of the t-SNAREs, whereas both t-SNAREs will localize to vertices when trans-pairing of SNAREs is blocked. Thus, trans-SNARE pairing is not required for SNARE vertex enrichment; and (d) The t-SNAREs regulate the vertex enrichment of both G-actin and the Ypt7p effector complex for homotypic fusion and vacuole protein sorting (HOPS). In accord with this hierarchy concept, the HOPS complex, at the end of the vertex assembly hierarchy, is most enriched at those vertices with abundant Ypt7p, which is at the start of the hierarchy. Our findings provide a unique view of the functional relationships between GTPases, SNAREs, and actin in membrane fusion.

Indexed as

Vesicular Transport ProteinsActinsCarrier ProteinsCells, CulturedGTP PhosphohydrolasesIntracellular MembranesMacromolecular SubstancesMembrane FusionMembrane ProteinsNerve Tissue ProteinsProtein Structure, TertiaryProtein TransportQa-SNARE ProteinsQb-SNARE Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsActinsCarrier ProteinsGTP PhosphohydrolasesMacromolecular SubstancesMembrane ProteinsNerve Tissue ProteinsQa-SNARE ProteinsQb-SNARE Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsSynaptosomal-Associated Protein 25VAM3 protein, S cerevisiaeVesicular Transport ProteinsVTI1 protein, S cerevisiaeYPT7 protein, S cerevisiae

Identifiers

PMID12566429
PMCPMC2172665
OpenAlexW2154195767

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.