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Related Experiment Video

Updated: Jul 10, 2026

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Synucleins in Neural Physiology: Understanding Endogenous Function to Better Contextualize Pathology.

Garrett D Sheehan¹, Jun B Ding^1,2

¹Department of Neurosurgery, Stanford University, Stanford, California, USA;

Annual Review of Neuroscience

|July 8, 2026

Summary

Alpha-synuclein, a protein linked to synucleinopathies, has diverse nonpathological neuronal functions beyond the synapse. Understanding its structure and normal roles is key to understanding disease vulnerability.

Keywords:

pre- and postsynaptic mechanisms synaptic plasticity synaptic transmission synucleinopathy synucleins vesicular release

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Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

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Last Updated: Jul 10, 2026

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

Area of Science:

Neuroscience
Molecular Biology
Biochemistry

Background:

Alpha-synuclein is primarily known for its role in synucleinopathies.
Its nonpathological functions are not fully understood.
It is considered a presynaptic protein with emerging roles beyond this compartment.

Purpose of the Study:

To review the structure and function of alpha-synuclein.
To integrate current literature on alpha-synuclein's diverse roles.
To highlight how normal functions relate to disease vulnerability.

Main Methods:

Literature review and integration of existing research.
Analysis of alpha-synuclein's structural domains and their functions.
Examination of evidence for both presynaptic and nonsynaptic roles.

Main Results:

Alpha-synuclein is an intrinsically disordered protein with distinct regions for membrane binding, vesicle clustering, and protein interactions.
It plays multiple roles in neurotransmission, including vesicle pool organization and recycling.
Evidence suggests roles in nonsynaptic membranes and extracellular vesicle secretion.

Conclusions:

Alpha-synuclein possesses multifaceted functions within and beyond neuronal synapses.
Its structural properties enable diverse interactions crucial for neuronal function.
Dysregulation or loss of these normal functions may contribute to synucleinopathies.