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Amyloid Fibrils

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Related Experiment Video

Updated: May 6, 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

Synphilin-1 modulates alpha-synuclein assembly, release and uptake.

Diana F Lázaro^1,2, Triana Amen^3,4, Ellen Gerhardt⁵

¹Department of Pathology and Laboratory Medicine, Institute on Aging and Center for Neurodegenerative Disease Research, Perelman School of Medicine at the University of Pennsylvania, Pennsylvania, PA, USA. diana.lazaro@pennmedicine.upenn.edu.

NPJ Parkinson'S Disease

|November 20, 2025

Summary

This summary is machine-generated.

Researchers modeled alpha-synuclein (aSyn) assemblies in cells using synphilin-1 (Sph1). This revealed distinct gel- and solid-like inclusions, offering new insights into Parkinson

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A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

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Last Updated: May 6, 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

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

Published on: November 25, 2022

Area of Science:

Neuroscience
Biochemistry
Cell Biology

Background:

Alpha-synuclein (aSyn) is intrinsically disordered, implicated in phase separation and neurodegenerative diseases like Parkinson's.
The precise function and pathological mechanisms of aSyn remain incompletely understood.

Purpose of the Study:

To model different alpha-synuclein (aSyn) assemblies in living cells.
To investigate the role of synphilin-1 (Sph1) in modulating aSyn aggregation and inclusion formation.

Main Methods:

Coexpression of modified aSyn and Sph1 variants in living cells to create distinct assemblies.
Characterization of aSyn-Sph1 inclusions using antibody recognition, proteinase K resistance, and protein mobility assays.
Manipulation of the VN-Sph1 + aSyn-VC interaction to control inclusion characteristics.

Main Results:

Distinct gel- and solid-like aSyn assemblies were modeled, differentiated by morphology, antibody binding, protease resistance, and mobility.
The VN-Sph1 + aSyn-VC interaction allowed modulation of inclusion size and number.
Formed inclusions contained lysosomes and AP-1 vesicles, consistent with observations in human brain tissue.

Conclusions:

Synphilin-1 plays a crucial role in modulating alpha-synuclein aggregation and inclusion formation.
The study provides novel insights into the mechanisms of aSyn aggregation and release.
Highlights the importance of aSyn-interacting proteins in synucleinopathies and their complex copathologies.