Evidence map›Paper›PMID 23897890›Full record

ArticleThe Journal of cell biology2013

The synaptobrevin homologue Snc2p recruits the exocyst to secretory vesicles by binding to Sec6p.

David Shen, Hua Yuan, Alex Hutagalung, Avani Verma, Daniel Kümmel, Xudong Wu, Karin Reinisch, James A McNew, Peter Novick

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

41 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
  8. Emerging Roles of Exocyst Complex in Fungi: A Review.Journal of fungi (Basel, Switzerland) · 2024
    Review
  9. Article
  10. Article
  11. The machinery of vesicle fusion.Current opinion in cell biology · 2023
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Integrative structure and function of the yeast exocyst complex.Protein science : a publication of the Protein Society · 2020
    Article
  19. The Role of Secretory Pathways inJournal of fungi (Basel, Switzerland) · 2020
    Review
  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

9 authors at 3 institutions in 1 country.

David ShenDepartment of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
Hua Yuan
Alex Hutagalung
Avani Verma
Daniel Kümmel
Xudong Wu
Karin Reinisch
James A McNew
Peter Novick
University of California, San Diego · USYale University · USRice University · US

Funding

GENETICS OF SECRETION IN YEASTR01GM035370 · NIGMS · YALE UNIVERSITY · PI PETER Jay NOVICK · 1985 to 2026
$7.0M
Coordination of membrane traffic through rab GEF and GAP cascadesR01GM082861 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI NOVICK, PETER JAY · 2008 to 2020
$4.4M
Regulatory Mechanisms in Membrane TraffickingR01GM080616 · NIGMS · YALE UNIVERSITY · PI REINISCH, KARIN M · 2007 to 2018
$4.1M
Genetics of Secretion in YeastR37GM035370 · NIGMS · YALE UNIVERSITY · PI NOVICK, PETER JAY · 2001 to 2010
$3.9M
Functional Reconstitution of Yeast ExocytosisR01GM071832 · NIGMS · RICE UNIVERSITY · PI MCNEW, JAMES A · 2006 to 2010
$1.4M
Biochemical analysis of the ER fusion protein allastinR01GM101377 · NIGMS · RICE UNIVERSITY · PI MCNEW, JAMES A · 2012 to 2015
$1.1M
NIGMS NIH HHS GM071832NIGMS NIH HHS GM082861NIGMS NIH HHS GM35370NIGMS NIH HHS R01 GM035370NIGMS NIH HHS R01 GM071832NIGMS NIH HHS R01 GM080616NIGMS NIH HHS R01 GM082861NIGMS NIH HHS R01 GM101377NIGMS NIH HHS R37 GM035370
6 · The paper itself

Abstract

A screen for mutations that affect the recruitment of the exocyst to secretory vesicles identified genes encoding clathrin and proteins that associate or colocalize with clathrin at sites of endocytosis. However, no significant colocalization of the exocyst with clathrin was seen, arguing against a direct role in exocyst recruitment. Rather, these components are needed to recycle the exocytic vesicle SNAREs Snc1p and Snc2p from the plasma membrane into new secretory vesicles where they act to recruit the exocyst. We observe a direct interaction between the exocyst subunit Sec6p and the latter half of the SNARE motif of Snc2p. An snc2 mutation that specifically disrupts this interaction led to exocyst mislocalization and a block in exocytosis in vivo without affecting liposome fusion in vitro. Overexpression of Sec4p partially suppressed the exocyst localization defects of mutations in clathrin and clathrin-associated components. We propose that the exocyst is recruited to secretory vesicles by the combinatorial signals of Sec4-GTP and the Snc proteins. This could help to confer both specificity and directionality to vesicular traffic.

Indexed as

ExocytosisBinding SitesProtein BindingR-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory VesiclesVesicular Transport ProteinsR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSEC6 protein, S cerevisiaeSNC2 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID23897890
PMCPMC3734085
OpenAlexW2076970936

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.