Evidence map›Paper›PMID 22992751›Full record

ArticleBioarchitecture

Tethering factor P115: a new model for tether-SNARE interactions.

Robert Grabski, Jesse Hay, Elizabeth Sztul

Open access · bronzeAbstract readComment
In one paragraph

Article in Bioarchitecture. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Review
  3. Acute depletion of diacylglycerol from theJournal of lipid research · 2018
    Article
  4. Article
  5. Membrane tethering.F1000prime reports · 2014
    Review
  6. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 3 institutions in 1 country.

Robert GrabskiDepartment of Cell Biology, Developmental and Integrative; University of Alabama at Birmingham; Birmingham, AL USA.
Jesse HayDivision of Biological Sciences and Center for Structural and Functional Neuroscience; University of Montana; Missoula, MT USA.
Elizabeth SztulDepartment of Cell Biology, Developmental and Integrative; University of Alabama at Birmingham; Birmingham, AL USA.
St. Vincent's Birmingham · USUniversity of Alabama at Birmingham · USUniversity of Montana · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The membrane tethering factor p115 has been shown to have important functions in ER to Golgi traffic and Golgi biogenesis. The multidomain structure of p115 allows for interactions with a diverse array of proteins that govern cargo movement at the ER-Golgi interface. Within its C-terminal region p115 contains four coiled-coil domains (CC1-CC4). Of the four coiled-coils, only CC1 has been shown to be required for p115 function, presumably by its ability to bind numerous SNARE proteins as well as the small GTPase Rab1. Recently, we showed that CC4 also interacts with SNARE proteins and that CC4 is required for p115 function in Golgi homeostasis and the trafficking of transmembrane but not soluble cargo. Here, we propose a novel model wherein p115 facilitates membrane tethering and fusion by simultaneously engaging its CC1 and CC4 domains with distinct SNARE proteins to promote formation of SNARE complexes.

Indexed as

AnimalsCaenorhabditis elegansCell MembraneGolgi ApparatusVesicular Transport ProteinsVesicular Transport Proteinscoiled-coil domainGolgip115SNAREtethering

Identifiers

PMID22992751
PMCPMC3696062
OpenAlexW2047551993

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.