Evidence map›Paper›PMID 23051737›Full record

ArticleMolecular biology of the cell2012

Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.

Braden T Lobingier, Alexey J Merz

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 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

64 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Phagocytosis at a glance.Journal of cell science · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Emerging Concepts in Defective Macrophage Phagocytosis in Cystic Fibrosis.International journal of molecular sciences · 2022
    Review
  12. Article
  13. Article
  14. The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

4 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

2 authors at 1 institution in 1 country.

Braden T LobingierDepartment of Biochemistry, University of Washington, Seattle, WA 98195-3750, USA.
Alexey J Merz
University of Washington · US

Funding

TRAINING IN MOLECULAR AND CELLULAR BIOLOGYT32GM007270 · NIGMS · UNIVERSITY OF WASHINGTON · PI RAIBLE, DAVID W · 1985 to 2020
$21.0M
Dynamics of Endomembrane Docking and FusionR01GM077349 · NIGMS · UNIVERSITY OF WASHINGTON · PI MERZ, ALEXEY JARRELL · 2006 to 2024
$6.1M
NIGMS NIH HHS GM077349NIGMS NIH HHS R01 GM077349NIGMS NIH HHS T32 GM007270NIGMS NIH HHS T32 GM07270
6 · The paper itself

Abstract

Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins catalyze membrane fusion events in the secretory and endolysosomal systems, and all SNARE-mediated fusion processes require cofactors of the Sec1/Munc18 (SM) family. Vps33 is an SM protein and subunit of the Vps-C complexes HOPS (homotypic fusion and protein sorting) and CORVET (class C core vacuole/endosome tethering), which are central regulators of endocytic traffic. Here we present biochemical studies of interactions between Saccharomyces cerevisiae vacuolar SNAREs and the HOPS holocomplex or Vps33 alone. HOPS binds the N-terminal H(abc) domain of the Qa-family SNARE Vam3, but Vps33 is not required for this interaction. Instead, Vps33 binds the SNARE domains of Vam3, Vam7, and Nyv1. Vps33 directly binds vacuolar quaternary SNARE complexes, and the affinity of Vps33 for SNARE complexes is greater than for individual SNAREs. Through targeted mutational analyses, we identify missense mutations of Vps33 that produce a novel set of defects, including cargo missorting and the loss of Vps33-HOPS association. Together these data suggest a working model for membrane docking: HOPS associates with N-terminal domains of Vam3 and Vam7 through Vps33-independent interactions, which are followed by binding of Vps33, the HOPS SM protein, to SNARE domains and finally to the quaternary SNARE complex. Our results also strengthen the hypothesis that SNARE complex binding is a core attribute of SM protein function.

Indexed as

VacuolesEndosomesMembrane ProteinsMunc18 ProteinsMutation, MissenseProtein BindingProtein TransportQa-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsSynaptosomal-Associated Protein 25Vesicular Transport ProteinsMembrane ProteinsMunc18 ProteinsQa-SNARE ProteinsSaccharomyces cerevisiae ProteinsSEC1 protein, S cerevisiaeSNARE ProteinsSynaptosomal-Associated Protein 25VAM3 protein, S cerevisiaeVAM7 protein, S cerevisiaeVesicular Transport ProteinsVPS33 protein, S cerevisiae

Identifiers

PMID23051737
PMCPMC3510022
OpenAlexW2104969134

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.