Evidence map›Paper›PMID 20462954›Full record

ArticleMolecular biology of the cell2010

HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly.

Christopher M Hickey, William Wickner

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
5.7field-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

96 citing papers in PubMed, 137 citations in OpenAlex.

  1. Article
  2. Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025
    Article
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  9. PI3P regulates multiple stages of membrane fusion.Molecular biology of the cell · 2023
    Article
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  11. Review
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  16. Article
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36 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

2 authors at 1 institution in 1 country.

Christopher M HickeyDepartment of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
William Wickner
Dartmouth 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
Molecular and Cellular Biology at DartmouthT32GM008704 · NIGMS · DARTMOUTH COLLEGE · PI COMPTON, DUANE A. · 1998 to 2018
$6.8M
AUTOIMMUNITY &CONNECTIVE TISSUE BIOLOGY TRAININGT32AR007576 · NIAMS · DARTMOUTH COLLEGE · PI RIGBY, WILLIAM FREDERICK CARSON · 1994 to 2008
$1.7M
NIAMS NIH HHS T32 AR007576NIAMS NIH HHS T32AR-007576NIGMS NIH HHS R01 GM023377NIGMS NIH HHS R01GM-23377NIGMS NIH HHS T32 GM008704NIGMS NIH HHS T32GM-008704
6 · The paper itself

Abstract

Vacuole homotypic fusion has been reconstituted with all purified components: vacuolar lipids, four soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins, Sec17p, Sec18p, the Rab Ypt7p, and the hexameric homotypic fusion and vacuole protein sorting complex (HOPS). HOPS is a Rab-effector with direct affinity for SNAREs (presumably via its Sec1-Munc18 homologous subunit Vps33p) and for certain vacuolar lipids. Each of these pure vacuolar proteins was required for optimal proteoliposome clustering, raising the question of which was most directly involved. We now present model subreactions of clustering and fusion that reveal that HOPS is the direct agent of tethering. The Rab and vacuole lipids contribute to tethering by supporting the membrane association of HOPS. HOPS indirectly facilitates trans-SNARE complex formation by tethering membranes, because the synthetic liposome tethering factor polyethylene glycol can also stimulate trans-SNARE complex formation and fusion. SNAREs further stabilize the associations of HOPS-tethered membranes. HOPS then protects newly formed trans-SNARE complexes from disassembly by Sec17p/Sec18p.

Indexed as

Membrane FusionCell MembraneIntracellular MembranesLiposomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsVacuolesLiposomesSaccharomyces cerevisiae ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins

Identifiers

PMID20462954
PMCPMC2893992
OpenAlexW2130155363

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.