Evidence map›Paper›PMID 19776355›Full record

ArticleMolecular biology of the cell2009

Yeast Sec1p functions before and after vesicle docking.

Kristina Hashizume, Yi-Shan Cheng, Jenna L Hutton, Chi-Hua Chiu, Chavela M Carr

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Emerging Roles of Exocyst Complex in Fungi: A Review.Journal of fungi (Basel, Switzerland) · 2024
    Review
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  11. SM protein Munc18-2 facilitates transition of Syntaxin 11-mediated lipid mixing to complete fusion for T-lymphocyte cytotoxicity.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Structural basis of Vps33A recruitment to the human HOPS complex by Vps16.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  18. Article
  19. Article
  20. 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

5 authors at 2 institutions in 1 country.

Kristina HashizumeDepartment of Pathology and Laboratory Medicine, University of Medicine and Dentistry, New Jersey-Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.
Yi-Shan Cheng
Jenna L Hutton
Chi-Hua Chiu
Chavela M Carr
Johnson University · USRutgers, The State University of New Jersey · US

Funding

Molecular Mechanism of Sec1p-Regulated Membrane FusionR01GM066291 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI CARR, CHAVELA M · 2002 to 2007
$1.2M
NIGMS NIH HHS R01 GM066291NIGMS NIH HHS R01GM-066291
6 · The paper itself

Abstract

Sec1/Munc18 (SM) proteins bind cognate soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes and stimulate vesicle membrane fusion. Before fusion, vesicles are docked to specific target membranes. Regulation of vesicle docking is attributed to some but not all SM proteins, suggesting specialization of this earlier function. Yeast Sec1p seems to function only after vesicles are docked and SNARE complexes are assembled. Here, we show that yeast Sec1p is required before and after SNARE complex assembly, in support of general requirements for SM proteins in both vesicle docking and fusion. Two classes of sec1 mutants were isolated. Class A mutants are tightly blocked in cell growth and secretion at a step before SNARE complex assembly. Class B mutants have a SNARE complex binding defect, with a range in severity of cell growth and secretion defects. Mapping the mutations onto an SM protein structure implicates a peripheral bundle of helices for the early, docking function and a deep groove, opposite the syntaxin-binding cleft on nSec1/Munc-18, for the interaction between Sec1p and the exocytic SNARE complex.

Indexed as

Saccharomyces cerevisiaeAmino Acid SequenceAnimalsCytoplasmic VesiclesHumansMembrane FusionModels, MolecularMolecular Sequence DataMunc18 ProteinsMutagenesisProtein Structure, TertiarySaccharomyces cerevisiae ProteinsSequence AlignmentSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsMunc18 ProteinsSaccharomyces cerevisiae ProteinsSEC1 protein, S cerevisiaeSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins

Identifiers

PMID19776355
PMCPMC2777098
OpenAlexW2051766074

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.