Evidence map›Paper›PMID 9545229›Full record

ArticleThe EMBO journal1998

Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins.

X Cao, N Ballew, C Barlowe

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers.

0numbers the graph read from it
0cells of the map it votes in
159citing papers in PubMed
14.6field-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

159 citing papers in PubMed, 370 citations in OpenAlex.

  1. Article
  2. Article
  3. SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023
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  7. Review
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  12. Article
  13. The Role of Secretory Pathways inJournal of fungi (Basel, Switzerland) · 2020
    Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

99 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

3 authors at 1 institution in 1 country.

X CaoDepartment of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
N Ballew
C Barlowe
Dartmouth College · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ER-to-Golgi transport in yeast may be reproduced in vitro with washed membranes, purified proteins (COPII, Uso1p and LMA1) and energy. COPII coated vesicles that have budded from the ER are freely diffusible but then dock to Golgi membranes upon the addition of Uso1p. LMA1 and Sec18p are required for vesicle fusion after Uso1p function. Here, we report that the docking reaction is sensitive to excess levels of Sec19p (GDI), a treatment that removes the GTPase, Ypt1p. Once docked, however, vesicle fusion is no longer sensitive to GDI. In vitro binding experiments demonstrate that the amount of Uso1p associated with membranes is reduced when incubated with GDI and correlates with the level of membrane-bound Ypt1p, suggesting that this GTPase regulates Uso1p binding to membranes. To determine the influence of SNARE proteins on the vesicle docking step, thermosensitive mutations in Sed5p, Bet1p, Bos1p and Sly1p that prevent ER-to-Golgi transport in vitro at restrictive temperatures were employed. These mutations do not interfere with Uso1p-mediated docking, but block membrane fusion. We propose that an initial vesicle docking event of ER-derived vesicles, termed tethering, depends on Uso1p and Ypt1p but is independent of SNARE proteins.

Indexed as

Guanine Nucleotide Dissociation Inhibitorsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAnimalsBiological TransportCarrier ProteinsCoated VesiclesEndoplasmic Reticulum, RoughFungal ProteinsGlycoproteinsGolgi ApparatusGTP-Binding ProteinsGTP PhosphohydrolasesMembrane FusionMembrane ProteinsBET1 protein, Zea maysBOS1 protein, S cerevisiaeCarrier ProteinsFungal ProteinsGDP dissociation inhibitor 1GlycoproteinsGTP-Binding ProteinsGTP PhosphohydrolasesGuanine Nucleotide Dissociation InhibitorsMembrane ProteinsMunc18 ProteinsPlant ProteinsQa-SNARE ProteinsQb-SNARE Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSed5 protein, S cerevisiaeSLY1 protein, S cerevisiaeSNARE ProteinsThioredoxinsUSO1 protein, S cerevisiaeVesicular Transport Proteinsyeast proteinase B inhibitorYPT1 protein, S cerevisiae

Identifiers

PMID9545229
PMCPMC1170560
OpenAlexW2009644279

What OpenQuestion holds

Textmetadata
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.