Evidence map›Paper›PMID 19073882›Full record

ArticleMolecular biology of the cell2009

Sec6p anchors the assembled exocyst complex at sites of secretion.

Jennifer A Songer, Mary Munson

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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 48 citations in OpenAlex.

  1. Emerging Roles of Exocyst Complex in Fungi: A Review.Journal of fungi (Basel, Switzerland) · 2024
    Review
  2. Article
  3. Article
  4. Integrative structure and function of the yeast exocyst complex.Protein science : a publication of the Protein Society · 2020
    Article
  5. Article
  6. Exposing the Elusive Exocyst Structure.Trends in biochemical sciences · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. CAPS and Munc13: CATCHRs that SNARE Vesicles.Frontiers in endocrinology · 2013
    Review
  16. Article
  17. Article
  18. Exorcising the exocyst complex.Traffic (Copenhagen, Denmark) · 2012
    Review
  19. Evolution of the land plant exocyst complexes.Frontiers in plant science · 2012
    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

2 authors at 1 institution in 1 country.

Jennifer A SongerDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Mary Munson
University of Massachusetts Chan Medical School · 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

The exocyst is an essential protein complex required for targeting and fusion of secretory vesicles to sites of exocytosis at the plasma membrane. To study the function of the exocyst complex, we performed a structure-based mutational analysis of the Saccharomyces cerevisiae exocyst subunit Sec6p. Two "patches" of highly conserved residues are present on the surface of Sec6p; mutation of either patch does not compromise protein stability. Nevertheless, replacement of SEC6 with the patch mutants results in severe temperature-sensitive growth and secretion defects. At nonpermissive conditions, although trafficking of secretory vesicles to the plasma membrane is unimpaired, none of the exocyst subunits are polarized. This is consistent with data from other exocyst temperature-sensitive mutants, which disrupt the integrity of the complex. Surprisingly, however, these patch mutations result in mislocalized exocyst complexes that remain intact. Our results indicate that assembly and polarization of the exocyst are functionally separable events, and that Sec6p is required to anchor exocyst complexes at sites of secretion.

Indexed as

AllelesAmino AcidsAmino Acid SequenceCarrier ProteinsConserved SequenceExosomesModels, MolecularMolecular Sequence DataMutant ProteinsMutationProtein BindingProtein SubunitsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAmino AcidsCarrier ProteinsMutant ProteinsProtein SubunitsSaccharomyces cerevisiae ProteinsSEC6 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID19073882
PMCPMC2633393
OpenAlexW2158237079

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.