Evidence map›Paper›PMID 22114349›Full record

ArticleMolecular biology of the cell2012

Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1.

Francesca Morgera, Margaret R Sallah, Michelle L Dubuke, Pallavi Gandhi, Daniel N Brewer, Chavela M Carr, Mary Munson

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. Article
  3. The exocyst in context.Biochemical Society transactions · 2024
    Review
  4. Emerging Roles of Exocyst Complex in Fungi: A Review.Journal of fungi (Basel, Switzerland) · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Exocytosis in Astrocytes.Biomolecules · 2021
    Review
  11. Plasma membrane phospholipid signature recruits the plant exocyst complex via the EXO70A1 subunit.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Chaperoning SNARE Folding and Assembly.Annual review of biochemistry · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Integrative structure and function of the yeast exocyst complex.Protein science : a publication of the Protein Society · 2020
    Article
  19. Article
  20. Article

3 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

7 authors at 2 institutions in 1 country.

Francesca MorgeraDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Margaret R Sallah
Michelle L Dubuke
Pallavi Gandhi
Daniel N Brewer
Chavela M Carr
Mary Munson
University of Massachusetts Chan Medical School · USTexas A&M University · US

Funding

Structure and Function of the Exocyst ComplexR01GM068803 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MUNSON, MARY · 2005 to 2021
$7.4M
NIGMS NIH HHS GM068803NIGMS NIH HHS R01 GM068803
6 · The paper itself

Abstract

Trafficking of protein and lipid cargo through the secretory pathway in eukaryotic cells is mediated by membrane-bound vesicles. Secretory vesicle targeting and fusion require a conserved multisubunit protein complex termed the exocyst, which has been implicated in specific tethering of vesicles to sites of polarized exocytosis. The exocyst is directly involved in regulating soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE) complexes and membrane fusion through interactions between the Sec6 subunit and the plasma membrane SNARE protein Sec9. Here we show another facet of Sec6 function-it directly binds Sec1, another SNARE regulator, but of the Sec1/Munc18 family. The Sec6-Sec1 interaction is exclusive of Sec6-Sec9 but compatible with Sec6-exocyst assembly. In contrast, the Sec6-exocyst interaction is incompatible with Sec6-Sec9. Therefore, upon vesicle arrival, Sec6 is proposed to release Sec9 in favor of Sec6-exocyst assembly and to simultaneously recruit Sec1 to sites of secretion for coordinated SNARE complex formation and membrane fusion.

Indexed as

ExocytosisMembrane FusionMunc18 ProteinsProtein SubunitsQc-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsVesicular Transport ProteinsMunc18 ProteinsProtein SubunitsQc-SNARE ProteinsSaccharomyces cerevisiae ProteinsSEC1 protein, S cerevisiaeSEC6 protein, S cerevisiaeSEC9 protein, S cerevisiaeSNARE ProteinsVesicular Transport Proteins

Identifiers

PMID22114349
PMCPMC3258177
OpenAlexW2101011089

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.