Evidence map›Paper›PMID 10385523›Full record

ArticleThe Journal of cell biology1999

Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion.

C Ungermann, G F von Mollard, O N Jensen, N Margolis, T H Stevens, W Wickner

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
6.7field-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

80 citing papers in PubMed, 163 citations in OpenAlex.

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20 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

6 authors at 3 institutions in 2 countries.

C UngermannDepartment of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755-3844, USA.
G F von Mollard
O N Jensen
N Margolis
T H Stevens
W Wickner
University of Oregon · USUniversity of Göttingen · DEDartmouth College · US

Funding

THE ASSEMBLY OF PROTEINS INTO BIOLOGICAL MEMBRANESR01GM023377 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WICKNER, WILLIAM TOBEY · 1985 to 2015
$17.9M
Cell Biological Study of Eukaryotic Organelle AssemblyR37GM032448 · NIGMS · UNIVERSITY OF OREGON · PI STEVENS, TOM HALL · 2003 to 2012
$3.6M
CELL BIOLOGICAL STUDY OF EUKARYOTIC ORGANELLE ASSEMBLYR01GM032448 · NIGMS · UNIVERSITY OF OREGON · PI STEVENS, TOM HALL · 1985 to 2002
$970k
THE ASSEMBLY OF PROTEINS INTO BIOLOGICAL MEMBRANESR37GM023377 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WICKNER, WILLIAM TOBEY · 1988 to 1997
–
NIGMS NIH HHS GM23377NIGMS NIH HHS GM32448NIGMS NIH HHS R01 GM023377NIGMS NIH HHS R01 GM032448NIGMS NIH HHS R37 GM032448
6 · The paper itself

Abstract

Vacuole SNAREs, including the t-SNAREs Vam3p and Vam7p and the v-SNARE Nyv1p, are found in a multisubunit "cis" complex on isolated organelles. We now identify the v-SNAREs Vti1p and Ykt6p by mass spectrometry as additional components of the immunoisolated vacuolar SNARE complex. Immunodepletion of detergent extracts with anti-Vti1p removes all the Ykt6p that is in a complex with Vam3p, immunodepletion with anti-Ykt6p removes all the Vti1p that is complexed with Vam3p, and immunodepletion with anti-Nyv1p removes all the Ykt6p in complex with other SNAREs, demonstrating that they are all together in the same cis multi-SNARE complex. After priming, which disassembles the cis-SNARE complex, antibodies to any of the five SNARE proteins still inhibit the fusion assay until the docking stage is completed, suggesting that each SNARE plays a role in docking. Furthermore, vti1 temperature-sensitive alleles cause a synthetic fusion-defective phenotype in our reaction. Our data show that vacuole-vacuole fusion requires a cis-SNARE complex of five SNAREs, the t-SNAREs Vam3p and Vam7p and the v-SNAREs Nyv1p, Vti1p, and Ykt6p.

Indexed as

Membrane FusionSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAllelesAntibodiesCarrier ProteinsChromatography, AffinityFungal ProteinsIntracellular MembranesMembrane ProteinsNerve Tissue ProteinsN-Ethylmaleimide-Sensitive ProteinsNuclear ProteinsPhenotypePrecipitin TestsProtein BindingAntibodiesCarrier ProteinsFungal ProteinsMembrane ProteinsNerve Tissue ProteinsN-Ethylmaleimide-Sensitive ProteinsNuclear ProteinsQa-SNARE ProteinsQb-SNARE ProteinsReceptors, Cytoplasmic and NuclearR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsSynaptosomal-Associated Protein 25VAM3 protein, S cerevisiaeVesicular Transport ProteinsVTI1 protein, S cerevisiaeYKT6 protein, S cerevisiae

Identifiers

PMID10385523
PMCPMC2133161
OpenAlexW2030468686

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.