Evidence map›Paper›PMID 38951706›Full record

ArticleNature cell biology2024

VAMP2 chaperones α-synuclein in synaptic vesicle co-condensates.

Chuchu Wang, Kai Zhang, Bin Cai, Jillian E Haller, Kathryn E Carnazza, Jiaojiao Hu, Chunyu Zhao, Zhiqi Tian, Xiao Hu, Daniel Hall and 12 more

Abstract read
In one paragraph

Article in Nature cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. The disordered and structured regions ofbioRxiv : the preprint server for biology · 2026
    Article
  14. Review
  15. Article
  16. Article
  17. A Novel α-Synuclein K58N Missense Variant in a Patient with Parkinson's Disease.Movement disorders : official journal of the Movement Disorder Society · 2025
    Article
  18. Review
  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

22 authors.

Chuchu WangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0003-2015-7331
Kai ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Bin CaiDepartment of Cancer Biology, University of Cincinnati College of Medicine, Cincinnati, OH, USA.
Jillian E HallerHelen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY, USA.
Kathryn E CarnazzaHelen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY, USA.
Jiaojiao HuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Chunyu ZhaoInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0003-0168-2130
Zhiqi TianDepartment of Cancer Biology, University of Cincinnati College of Medicine, Cincinnati, OH, USA.
Xiao HuDepartment of Cancer Biology, University of Cincinnati College of Medicine, Cincinnati, OH, USA.
Daniel HallDepartment of Cancer Biology, University of Cincinnati College of Medicine, Cincinnati, OH, USA.
Jiali QiangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Shouqiao HouInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Zhenying LiuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Jinge GuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Yaoyang ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0001-5363-9834
Kim B SeroogyDepartment of Neurology, University of Cincinnati College of Medicine, Cincinnati, OH, USA.
Jacqueline BurréHelen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY, USA.ORCID http://orcid.org/0000-0001-8968-248X
Yanshan FangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0002-4123-0174
Cong LiuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0003-3425-6672
Axel T BrungerDepartment of Molecular and Cellular Physiology, Stanford University, Stanford, CA, USA.ORCID http://orcid.org/0000-0001-5121-2036
Dan LiBio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders (Ministry of Education), Shanghai Jiao Tong University, Shanghai, China. lidan2017@sjtu.edu.cn.ORCID http://orcid.org/0000-0002-1609-1539
Jiajie DiaoDepartment of Cancer Biology, University of Cincinnati College of Medicine, Cincinnati, OH, USA. jiajie.diao@uc.edu.ORCID http://orcid.org/0000-0003-4288-3203

Funding

The impact of synaptic vesicle-binding of alpha-synuclein on neuron function and neuropathologyR01NS113960 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BURRE, JACQUELINE · 2020 to 2024
$2.4M
The Impact of Beta- and Gamma-Synucleins on Alpha-Synuclein's Synaptic FunctionRF1NS126342 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BURRE, JACQUELINE, SHARMA, MANU · 2022 to 2023
$2.3M
The role of VAMP2 in alpha-synuclein function and pathologyR01NS121077 · NINDS · UNIVERSITY OF CINCINNATI · PI BURRE, JACQUELINE, DIAO, JIAJIE · 2021 to 2025
$1.9M
Molecular mechanisms of Munc18-1 linked infantile seizure disorders and rational rescue strategiesR01NS102181 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BURRE, JACQUELINE · 2017 to 2021
$1.8M
The Impact of Beta- and Gamma-Synucleins on Alpha-Synuclein's Synaptic FunctionR01NS126342 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI Jacqueline Burre, Manu Sharma · 2025 to 2026
$1.5M
Synaptic vesicle changes in synucleinopathiesR21NS127939 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BURRE, JACQUELINE · 2022 to 2022
$464k
NINDS NIH HHS R01 NS102181NINDS NIH HHS R01 NS113960NINDS NIH HHS R01 NS121077NINDS NIH HHS R01 NS126342NINDS NIH HHS R21 NS127939NINDS NIH HHS RF1 NS126342U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke (NINDS) R01NS121077
6 · The paper itself

Abstract

α-Synuclein (α-Syn) aggregation is closely associated with Parkinson's disease neuropathology. Physiologically, α-Syn promotes synaptic vesicle (SV) clustering and soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex assembly. However, the underlying structural and molecular mechanisms are uncertain and it is not known whether this function affects the pathological aggregation of α-Syn. Here we show that the juxtamembrane region of vesicle-associated membrane protein 2 (VAMP2)-a component of the SNARE complex that resides on SVs-directly interacts with the carboxy-terminal region of α-Syn through charged residues to regulate α-Syn's function in clustering SVs and promoting SNARE complex assembly by inducing a multi-component condensed phase of SVs, α-Syn and other components. Moreover, VAMP2 binding protects α-Syn against forming aggregation-prone oligomers and fibrils in these condensates. Our results suggest a molecular mechanism that maintains α-Syn's function and prevents its pathological amyloid aggregation, the failure of which may lead to Parkinson's disease.

Indexed as

alpha-SynucleinSynaptic VesiclesVesicle-Associated Membrane Protein 2AnimalsHumansMiceMolecular ChaperonesNeuronsParkinson DiseaseProtein BindingRatsSNARE Proteinsalpha-SynucleinMolecular ChaperonesSNARE ProteinsVAMP2 protein, humanVesicle-Associated Membrane Protein 2vesicle-associated membrane protein 2, mouse

Identifiers

PMID38951706
PMCPMC11786254

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.