Evidence map›Paper›PMID 25406594›Full record

ArticleTraffic (Copenhagen, Denmark)2015

p115-SNARE interactions: a dynamic cycle of p115 binding monomeric SNARE motifs and releasing assembled bundles.

Ting Wang, Robert Grabski, Elizabeth Sztul, Jesse C Hay

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. IRAP Endosomes Control Phagosomal Maturation in Dendritic Cells.Frontiers in cell and developmental biology · 2020
    Article
  8. Review
  9. Golgi Structure and Function in Health, Stress, and Diseases.Results and problems in cell differentiation · 2019
    Review
  10. Article
  11. The Journal of cell biology · 2017
    Article
  12. Article
  13. Chaperoning SNARE assembly and disassembly.Nature reviews. Molecular cell biology · 2016
    Review
  14. Coat/Tether Interactions-Exception or Rule?Frontiers in cell and developmental biology · 2016
    Review
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

4 authors at 2 institutions in 1 country.

Ting WangDivision of Biological Sciences and Center for Structural & Functional Neuroscience, The University of Montana, Missoula, MT, USA.
Robert Grabski
Elizabeth Sztul
Jesse C Hay
University of Alabama at Birmingham · USUniversity of Montana · US

Funding

PROTEIN INTERACTIONS CONTROLLING ER/GOLGI TRANSPORTR01GM059378 · NIGMS · UNIVERSITY OF MONTANA · PI HAY, JESSE C · 1999 to 2010
$2.2M
Regulation of ER to Golgi Transport byLuminal CalciumR15GM106323 · NIGMS · UNIVERSITY OF MONTANA · PI HAY, JESSE C · 2013 to 2022
$1.3M
NIGMS NIH HHS GM106323NIGMS NIH HHS GM59378NIGMS NIH HHS R01 GM059378NIGMS NIH HHS R15 GM106323
6 · The paper itself

Abstract

Tethering factors regulate the targeting of membrane-enclosed vesicles under the control of Rab GTPases. p115, a golgin family tether, has been shown to participate in multiple stages of ER/Golgi transport. Despite extensive study, the mechanism of action of p115 is poorly understood. SNARE proteins make up the machinery for membrane fusion, and strong evidence shows that function of p115 is directly linked to its interaction with SNAREs. Using a gel filtration binding assay, we have demonstrated that in solution p115 stably interacts with ER/Golgi SNAREs rbet1 and sec22b, but not membrin and syntaxin 5. These binding preferences stemmed from selectivity of p115 for monomeric SNARE motifs as opposed to SNARE oligomers. Soluble monomeric rbet1 can compete off p115 from coat protein II (COPII) vesicles. Furthermore, excess p115 inhibits p115 function in trafficking. We conclude that monomeric SNAREs are a major binding site for p115 on COPII vesicles, and that p115 dissociates from its SNARE partners upon SNAREpin assembly. Our results suggest a model in which p115 forms a mixed p115/SNARE helix bundle with a monomeric SNARE, facilitates the binding activity and/or concentration of the SNARE at prefusion sites and is subsequently ejected as SNARE complex formation and fusion proceed.

Indexed as

AnimalsBinding SitesCHO CellsCOP-Coated VesiclesCricetinaeCricetulusGolgi Matrix ProteinsProtein BindingProtein MultimerizationProtein TransportQc-SNARE ProteinsRatsR-SNARE ProteinsVesicular Transport ProteinsBET1 protein, ratGolgi Matrix ProteinsQc-SNARE ProteinsR-SNARE ProteinsSec22a protein, ratvesicular transport factor p115Vesicular Transport Proteinsbet1endoplasmic reticulum to Golgi transportmembrane fusionmembrane tethersp115sec22secretionSNAREsyntaxin 5vesicle transport

Identifiers

PMID25406594
PMCPMC4304910
OpenAlexW1843673884

What OpenQuestion holds

Textmetadata
LicenceTDM
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.