Evidence map›Paper›PMID 35417693›Full record

ArticleCell reports2022

Synaptic vesicle binding of α-synuclein is modulated by β- and γ-synucleins.

Kathryn E Carnazza, Lauren E Komer, Ying Xue Xie, André Pineda, Juan Antonio Briano, Virginia Gao, Yoonmi Na, Trudy Ramlall, Vladimir L Buchman, David Eliezer and 2 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Cell reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

39 citing papers in PubMed, 48 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 2 institutions in 3 countries.

Kathryn E CarnazzaHelen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY 10021, USA.
Lauren E KomerHelen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY 10021, USA.
Ying Xue XieHelen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY 10021, USA.
André PinedaHelen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY 10021, USA.
Juan Antonio BrianoHelen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY 10021, USA.
Virginia GaoHelen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY 10021, USA.
Yoonmi NaHelen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY 10021, USA.
Trudy RamlallDepartment of Biochemistry, Weill Cornell Medicine, New York, NY 10021, USA.
Vladimir L BuchmanSchool of Biosciences, Cardiff University, Cardiff CF103AX, UK; Belgorod State National Research University, 85 Pobedy Street, Belgorod, Belgorod 308015, Russian Federation.
David EliezerDepartment of Biochemistry, Weill Cornell Medicine, New York, NY 10021, USA.
Manu SharmaHelen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY 10021, USA.
Jacqueline BurréHelen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY 10021, USA. Electronic address: jab2058@med.cornell.edu.
Cornell University · USBelgorod National Research University · RU

Funding

Structure and Function of Protein Disorder in Membrane Trafficking and OrganizationR35GM136686 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI ELIEZER, DAVID · 2020 to 2025
$4.5M
Structure and Function of Alpha-SynucleinR37AG019391 · NIA · WEILL MEDICAL COLL OF CORNELL UNIV · PI ELIEZER, DAVID · 2010 to 2019
$3.4M
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
DnaJ co-chaperones which modify tau aggregation and neurodegenerationR01AG052505 · NIA · WEILL MEDICAL COLL OF CORNELL UNIV · PI SHARMA, MANU · 2016 to 2020
$1.9M
The role of VAMP2 in alpha-synuclein function and pathologyR01NS121077 · NINDS · UNIVERSITY OF CINCINNATI · PI BURRE, JACQUELINE, DIAO, JIAJIE · 2021 to 2025
$1.9M
Cellular mechanism of Adult Onset Neuronal Ceroid Lipofuscinosis (ANCL) caused by mutations in cysteine string protein-alpha (CSPalpha).R01NS095988 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI SHARMA, MANU · 2017 to 2021
$1.8M
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 role of beta-synuclein in synaptic vesicle releaseF31NS125949 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI KOMER, LAUREN · 2022 to 2023
$69k
NIA NIH HHS R01 AG052505NIA NIH HHS R37 AG019391NIGMS NIH HHS R35 GM136686NINDS NIH HHS F31 NS125949NINDS NIH HHS R01 NS095988NINDS NIH HHS R01 NS102181NINDS NIH HHS R01 NS113960NINDS NIH HHS R01 NS121077
6 · The paper itself

Abstract

α-synuclein, β-synuclein, and γ-synuclein are abundantly expressed proteins in the vertebrate nervous system. α-synuclein functions in neurotransmitter release by binding to and clustering synaptic vesicles and chaperoning SNARE-complex assembly. Pathologically, aggregates originating from soluble pools of α-synuclein are deposited into Lewy bodies in Parkinson's disease and related synucleinopathies. The functions of β-synuclein and γ-synuclein in presynaptic terminals remain poorly studied. Using in vitro liposome binding studies, circular dichroism spectroscopy, immunoprecipitation, and fluorescence resonance energy transfer (FRET) experiments on isolated synaptic vesicles in combination with subcellular fractionation of brains from synuclein mouse models, we show that β-synuclein and γ-synuclein have a reduced affinity toward synaptic vesicles compared with α-synuclein, and that heteromerization of β-synuclein or γ-synuclein with α-synuclein results in reduced synaptic vesicle binding of α-synuclein in a concentration-dependent manner. Our data suggest that β-synuclein and γ-synuclein are modulators of synaptic vesicle binding of α-synuclein and thereby reduce α-synuclein's physiological activity at the neuronal synapse.

Indexed as

alpha-SynucleinSynaptic VesiclesAnimalsbeta-Synucleingamma-SynucleinMicePresynaptic Terminalsalpha-Synucleinbeta-Synucleingamma-SynucleinCP: Neuroscienceinteractionmembrane bindingmultimersneurodegenerationParkinson’s diseasesynapsesynaptic vesiclesynucleinsynucleinopathy

Identifiers

PMID35417693
PMCPMC9116446
OpenAlexW4223950291

What OpenQuestion holds

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LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

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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.