Evidence map›Paper›PMID 32734583›Full record

ArticleCellular and molecular life sciences : CMLS2021

ORP/Osh mediate cross-talk between ER-plasma membrane contact site components and plasma membrane SNAREs.

Marion Weber-Boyvat, Thorsten Trimbuch, Saundarya Shah, Jussi Jäntti, Vesa M Olkkonen, Christian Rosenmund

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. The Endoplasmic Reticulum and Its Contacts: Emerging Roles in Axon Development, Neurotransmission, and Degeneration.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2024
    Review
  8. Review
  9. CaAdvances in experimental medicine and biology · 2023
    Article
  10. Review
  11. Review
  12. Review
  13. ER-PM Contact Sites - SNARING Actors in Emerging Functions.Frontiers in cell and developmental biology · 2021
    Review
  14. Review
  15. 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

6 authors at 4 institutions in 2 countries.

Marion Weber-BoyvatInstitute of Neurophysiology and NeuroCure Cluster of Excellence, Charité Universitätsmedizin Berlin, 10117, Berlin, Germany. marion.weber-boyvat@charite.de.ORCID http://orcid.org/0000-0002-3447-8294
Thorsten TrimbuchInstitute of Neurophysiology and NeuroCure Cluster of Excellence, Charité Universitätsmedizin Berlin, 10117, Berlin, Germany.
Saundarya ShahMinerva Foundation Institute for Medical Research, 00290, Helsinki, Finland.
Jussi JänttiVTT Technical Research Center of Finland, 02044 VTT, Espoo, Finland.
Vesa M OlkkonenMinerva Foundation Institute for Medical Research, 00290, Helsinki, Finland.
Christian RosenmundInstitute of Neurophysiology and NeuroCure Cluster of Excellence, Charité Universitätsmedizin Berlin, 10117, Berlin, Germany. christian.rosenmund@charite.de.
Charité - Universitätsmedizin Berlin · DEMinerva Foundation · FIUniversity of Helsinki · FIVTT Technical Research Centre of Finland · FI

Funding

Academy of Finland 257049Academy of Finland 285223 and 322647
6 · The paper itself

Abstract

OSBP-homologous proteins (ORPs, Oshp) are lipid binding/transfer proteins. Several ORP/Oshp localize to membrane contacts between the endoplasmic reticulum (ER) and the plasma membrane, where they mediate lipid transfer or regulate lipid-modifying enzymes. A common way in which they target contacts is by binding to the ER proteins, VAP/Scs2p, while the second membrane is targeted by other interactions with lipids or proteins.We have studied the cross-talk of secretory SNARE proteins and their regulators with ORP/Oshp and VAPA/Scs2p at ER-plasma membrane contact sites in yeast and murine primary neurons. We show that Oshp-Scs2p interactions depend on intact secretory SNARE proteins, especially Sec9p. SNAP-25/Sec9p directly interact with ORP/Osh proteins and their disruption destabilized the ORP/Osh proteins, associated with dysfunction of VAPA/Scs2p. Deleting OSH1-3 in yeast or knocking down ORP2 in primary neurons reduced the oligomerization of VAPA/Scs2p and affected their multiple interactions with SNAREs. These observations reveal a novel cross-talk between the machineries of ER-plasma membrane contact sites and those driving exocytosis.

Indexed as

AnimalsBiological TransportCarrier ProteinsCell MembraneEndoplasmic ReticulumExocytosisHumansLipid MetabolismMembrane ProteinsMiceOxysterol Binding ProteinsQc-SNARE ProteinsReceptors, SteroidSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsCarrier Proteinslipid transfer proteinMembrane ProteinsOSBPL2 protein, humanOxysterol Binding ProteinsQc-SNARE ProteinsReceptors, SteroidSaccharomyces cerevisiae ProteinsScs2 protein, S cerevisiaeSEC9 protein, S cerevisiaeSNARE ProteinsSterolsSWH1 protein, S cerevisiaeSynaptosomal-Associated Protein 25Vapa protein, mouseVesicular Transport ProteinsMembrane contact siteORPOshSec9SNAP-25SNARE

Identifiers

PMID32734583
PMCPMC7904734
OpenAlexW3046779589

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.