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Related Experiment Video

Updated: Sep 15, 2025

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Published on: August 16, 2020

Pathological α-Synuclein Perturbs Nuclear Integrity.

Michael Millett¹, Allison Comite¹, Elisabeth Martin Castosa¹

¹Department of Pharmacology & Therapeutics and Center for Translational Research in Neurodegeneration, University of Florida College of Medicine, Gainesville, FL 32610.

Biorxiv : the Preprint Server for Biology

|July 14, 2025

Summary

Pathological alpha-synuclein aggregates in the nucleus damage nuclear integrity and function in synucleinopathies. This nuclear pathology is linked to DNA damage and altered nuclear envelope repair, impacting cellular health.

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Area of Science:

Neuroscience
Cell Biology
Molecular Biology

Background:

Alpha-synuclein aggregates are key in synucleinopathies.
Its role in nuclear function remains controversial and poorly understood.
Existing research focuses on synaptic roles, neglecting nuclear implications.

Purpose of the Study:

To investigate the nuclear localization of pathological alpha-synuclein.
To determine the consequences of nuclear alpha-synuclein accumulation on nuclear integrity.
To explore the mechanistic impact on DNA damage, nuclear envelope, and RNA localization.

Main Methods:

Utilized synucleinopathy mouse and cell culture models.
Examined postmortem human Lewy Body Dementia brain tissue.
Employed quantitative super-resolution microscopy and molecular markers for DNA damage and nuclear envelope integrity.

Main Results:

Observed pathological alpha-synuclein aggregation within the nucleus in mouse models and human LBD cortex.
Nuclear alpha-synuclein correlated with abnormal nuclear morphology and increased DNA damage (53BP1).
Detected elevated nuclear envelope damage markers, altered repair marker expression, and changed RNA localization.

Conclusions:

Rigorously demonstrated nuclear localization of pathological alpha-synuclein using super-resolution microscopy.
Provided novel insights into the impact of nuclear alpha-synuclein on nuclear integrity and function.
Highlighted potential mechanisms linking nuclear pathology to disease progression in synucleinopathies.