Evidence map›Paper›PMID 11739408›Full record

ArticleThe Journal of cell biology2001

The Tlg SNARE complex is required for TGN homotypic fusion.

J H Brickner, J M Blanchette, G Sipos, R S Fuller

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 44 citations in OpenAlex.

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  17. t-SNARE phosphorylation regulates endocytosis in yeast.Molecular biology of the cell · 2002
    Article
  18. 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

4 authors at 1 institution in 1 country.

J H BricknerDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
J M Blanchette
G Sipos
R S Fuller
University of Michigan–Ann Arbor · US

Funding

PREDOCTORAL TRAINING IN GENETICST32GM007544 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MORAN, JOHN V. · 1985 to 2022
$11.3M
GOLGI TARGETING AND RETENTION OF YEAST KEX2 PROTEASER01GM050915 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI FULLER, ROBERTA S. · 1994 to 2009
$1.7M
NIGMS NIH HHS GM07544NIGMS NIH HHS GM50915NIGMS NIH HHS R01 GM050915NIGMS NIH HHS T32 GM007544
6 · The paper itself

Abstract

Using a new assay for membrane fusion between late Golgi/endosomal compartments, we have reconstituted a rapid, robust homotypic fusion reaction between membranes containing Kex2p and Ste13p, two enzymes resident in the yeast trans-Golgi network (TGN). Fusion was temperature, ATP, and cytosol dependent. It was inhibited by dilution, Ca+2 chelation, N-ethylmaleimide, and detergent. Coimmunoisolation confirmed that the reaction resulted in cointegration of the two enzymes into the same bilayer. Antibody inhibition experiments coupled with antigen competition indicated a requirement for soluble NSF attachment protein receptor (SNARE) proteins Tlg1p, Tlg2p, and Vti1p in this reaction. Membrane fusion also required the rab protein Vps21p. Vps21p was sufficient if present on either the Kex2p or Ste13p membranes alone, indicative of an inherent symmetry in the reaction. These results identify roles for a Tlg SNARE complex composed of Tlg1p, Tlg2p, Vti1p, and the rab Vps21p in this previously uncharacterized homotypic TGN fusion reaction.

Indexed as

Membrane Transport ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsCarrier ProteinsCell-Free SystemFucosyltransferasesGalactoside 2-alpha-L-fucosyltransferaseMembrane FusionMembrane ProteinsQa-SNARE ProteinsQb-SNARE Proteinsrab5 GTP-Binding Proteinsrab GTP-Binding ProteinsSNARE Proteinstrans-Golgi NetworkYeastsCarrier ProteinsFucosyltransferasesGalactoside 2-alpha-L-fucosyltransferaseMembrane ProteinsMembrane Transport ProteinsQa-SNARE ProteinsQb-SNARE Proteinsrab5 GTP-Binding Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsTLG2 protein, S cerevisiaeVesicular Transport ProteinsVTI1 protein, S cerevisiae

Identifiers

PMID11739408
PMCPMC2150899
OpenAlexW2138473874

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.