Evidence map›Paper›PMID 28495859›Full record

ArticleThe Biochemical journal2017

α-Synuclein may cross-bridge v-SNARE and acidic phospholipids to facilitate SNARE-dependent vesicle docking.

Xiaochu Lou, Jaewook Kim, Brenden J Hawk, Yeon-Kyun Shin

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

59 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Parkinson disease is a fatty acidopathy.Nature reviews. Neurology · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Molecular Dynamics Simulation for Membrane Fusion.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  10. Article
  11. Article
  12. From Synaptic Physiology to Synaptic Pathology: The Enigma of α-Synuclein.International journal of molecular sciences · 2024
    Review
  13. Review
  14. Frontiers in molecular neuroscience · 2024
    Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Xiaochu LouRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, U.S.A.
Jaewook KimRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, U.S.A.
Brenden J HawkRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, U.S.A.
Yeon-Kyun ShinRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, U.S.A. colishin@iastate.edu.
Iowa State University · US

Funding

Regulations of SNARE-dependent membrane fusionR01GM051290 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI SHIN, YEON-KYUN · 1999 to 2019
$5.0M
NIGMS NIH HHS R01 GM051290
6 · The paper itself

Abstract

Misfolded α-synuclein (A-syn) is widely recognized as the primal cause of neurodegenerative diseases including Parkinson's disease and dementia with Lewy bodies. The normal cellular function of A-syn has, however, been elusive. There is evidence that A-syn plays multiple roles in the exocytotic pathway in the neuron, but the underlying molecular mechanisms are unclear. A-syn has been known to interact with negatively charged phospholipids and with vesicle SNARE protein VAMP2. Using single-vesicle docking/fusion assays, we find that A-syn promotes SNARE-dependent vesicles docking significantly at 2.5 µM. When phosphatidylserine (PS) is removed from t-SNARE-bearing vesicles, the docking enhancement by A-syn disappears and A-syn instead acts as an inhibitor for docking. In contrast, subtraction of PS from the v-SNARE-carrying vesicles enhances vesicle docking even further. Moreover, when we truncate the C-terminal 45 residues of A-syn that participates in interacting with VAMP2, the promotion of vesicle docking is abrogated. Thus, the results suggest that the A-syn's interaction with v-SNARE through its C-terminal tail and its concurrent interaction with PS

Indexed as

Models, Biologicalalpha-SynucleinAmino Acid SubstitutionAnimalsHumansLiposomesMembrane FusionMicellesMutagenesis, Site-DirectedMutationNerve Tissue ProteinsPeptide FragmentsPhosphatidylserinesProtein Interaction Domains and MotifsRatsRecombinant Fusion Proteinsalpha-SynucleinLiposomesMicellesNerve Tissue ProteinsPeptide FragmentsPhosphatidylserinesRecombinant Fusion ProteinsSNAP25 protein, humanSNARE ProteinsSNCA protein, humanSTX1A protein, humanSynaptosomal-Associated Protein 25Synaptotagmin ISyntaxin 1Syt1 protein, ratVAMP2 protein, humanVesicle-Associated Membrane Protein 2exocytosismembrane fusionsingle moleculeSNARE proteinsα-synuclein

Identifiers

PMID28495859
PMCPMC5772654
OpenAlexW2612934990

What OpenQuestion holds

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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.