Evidence map›Paper›PMID 15889152›Full record

ArticleThe EMBO journal2005

Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion.

Kevin M Collins, Naomi L Thorngren, Rutilio A Fratti, William T Wickner

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

74 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
  2. Review
  3. Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. PI3P regulates multiple stages of membrane fusion.Molecular biology of the cell · 2023
    Article
  10. SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Tethering guides fusion-competentProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Review
  20. Article

14 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.

Kevin M CollinsDepartment of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
Naomi L Thorngren
Rutilio A Fratti
William T 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 T32 GM 08704
6 · The paper itself

Abstract

SNARE functions during membrane docking and fusion are regulated by Sec1/Munc18 (SM) chaperones and Rab/Ypt GTPase effectors. These functions for yeast vacuole fusion are combined in the six-subunit HOPS complex. HOPS facilitates Ypt7p nucleotide exchange, is a Ypt7p effector, and contains an SM protein. We have dissected the associations and requirements for HOPS, Ypt7p, and Sec17/18p during SNARE complex assembly. Vacuole SNARE complexes bind either Sec17p or the HOPS complex, but not both. Sec17p and its co-chaperone Sec18p disassemble SNARE complexes. Ypt7p regulates the reassembly of unpaired SNAREs with each other and with HOPS, forming HOPS.SNARE complexes prior to fusion. After HOPS.SNARE assembly, lipid rearrangements are still required for vacuole content mixing. Thus, Sec17p and HOPS have mutually exclusive interactions with vacuole SNAREs to mediate disruption of SNARE complexes or their assembly for docking and fusion. Sec17p may displace HOPS from SNAREs to permit subsequent rounds of fusion.

Indexed as

Carrier ProteinsGenes, ReporterMembrane ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsVacuolesVesicular Transport ProteinsCarrier ProteinsMembrane ProteinsSaccharomyces cerevisiae ProteinsSEC17 protein, S cerevisiaeSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsVesicular Transport Proteins

Identifiers

PMID15889152
PMCPMC1142591
OpenAlexW2018622809

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.