Evidence map›Paper›PMID 32467162›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

PI(4,5)P

Ilona Kondratiuk, Shrutee Jakhanwal, Jialin Jin, Udhayabhaskar Sathyanarayanan, Benjamin Kroppen, Ajaybabu V Pobbati, Anita Krisko, Uri Ashery, Michael Meinecke, Reinhard Jahn and 2 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Alterations of presynaptic proteins in autism spectrum disorder.Frontiers in molecular neuroscience · 2022
    Review
  5. Article
  6. Article
  7. 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

12 authors at 3 institutions in 3 countries.

Ilona KondratiukEuropean Neuroscience Institute Göttingen, University Medical Center Göttingen and the Max-Planck Society, 37077 Göttingen, Germany.ORCID 0000-0002-7740-8923
Shrutee JakhanwalDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Jialin JinEuropean Neuroscience Institute Göttingen, University Medical Center Göttingen and the Max-Planck Society, 37077 Göttingen, Germany.
Udhayabhaskar SathyanarayananEuropean Neuroscience Institute Göttingen, University Medical Center Göttingen and the Max-Planck Society, 37077 Göttingen, Germany.
Benjamin KroppenInstitute for Cellular Biochemistry, University Medical Center Göttingen, 37075 Göttingen, Germany.
Ajaybabu V PobbatiDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Anita KriskoDepartment of Experimental Neurodegeneration, University Medical Center Göttingen, 37073 Göttingen, Germany.
Uri AsherySchool of Neurobiology, Biochemistry and Biophysics, George S. Wise Faculty of Life Sciences, Sagol School of Neuroscience, Tel Aviv University, 6997801 Tel Aviv, Israel.
Michael MeineckeInstitute for Cellular Biochemistry, University Medical Center Göttingen, 37075 Göttingen, Germany.ORCID 0000-0003-1414-6951
Reinhard JahnDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.ORCID 0000-0003-1542-3498
Dirk FasshauerDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.ORCID 0000-0002-1040-4282
Ira MilosevicEuropean Neuroscience Institute Göttingen, University Medical Center Göttingen and the Max-Planck Society, 37077 Göttingen, Germany; imilose@gwdg.de.ORCID 0000-0001-6440-3763
Universitätsmedizin Göttingen · DEMax Planck Institute for Biophysical Chemistry · DETel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The functions of nervous and neuroendocrine systems rely on fast and tightly regulated release of neurotransmitters stored in secretory vesicles through SNARE-mediated exocytosis. Few proteins, including tomosyn (STXBP5) and amisyn (STXBP6), were proposed to negatively regulate exocytosis. Little is known about amisyn, a 24-kDa brain-enriched protein with a SNARE motif. We report here that full-length amisyn forms a stable SNARE complex with syntaxin-1 and SNAP-25 through its C-terminal SNARE motif and competes with synaptobrevin-2/VAMP2 for the SNARE-complex assembly. Furthermore, amisyn contains an N-terminal pleckstrin homology domain that mediates its transient association with the plasma membrane of neurosecretory cells by binding to phospholipid PI(4,5)P

Indexed as

ExocytosisAnimalsCell MembraneCells, CulturedChromaffin CellsHumansLiposomesMembrane FusionPC12 CellsPhosphatidylinositol 4,5-DiphosphatePleckstrin Homology DomainsProtein BindingRatsSNARE ProteinsSynaptosomal-Associated Protein 25Syntaxin 1LiposomesPhosphatidylinositol 4,5-DiphosphateSNAP25 protein, humanSNARE ProteinsStxbp6 protein, ratSynaptosomal-Associated Protein 25Syntaxin 1Vamp2 protein, ratVesicle-Associated Membrane Protein 2Vesicular Transport Proteinsautism spectrum disordersexocytosis inhibitionPI(4,5)P2SNARE complextomosyn

Identifiers

PMID32467162
PMCPMC7306819
OpenAlexW3030338221

What OpenQuestion holds

Textmetadata
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.