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Updated: Mar 24, 2026

Optogenetic Phase Transition of TDP-43 in Spinal Motor Neurons of Zebrafish Larvae

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Altered mRNP granule dynamics in FTLD pathogenesis.

Hilary A Bowden¹, Dorothee Dormann^2,1,3

¹Graduate School of Systemic Neurosciences (GSN), Planegg-Martinsried, Germany.

Journal of Neurochemistry

|March 4, 2016

Summary

This summary is machine-generated.

RNA-binding proteins (RBPs) in neurons can form pathological aggregates, leading to neurodegeneration. Dynamic mRNP granules may convert into these toxic aggregates, disrupting neuronal function.

Keywords:

ALS FTLD FUS/TLS TDP-43 mRNP granules stress granules

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Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models

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Published on: March 24, 2019

Area of Science:

Neuroscience
Molecular Biology
Genetics

Background:

RNA-binding proteins (RBPs) regulate gene expression in neurons, impacting processes like splicing and translation.
Defective or mislocalized RBPs are linked to neurodegenerative diseases, including frontotemporal lobar degeneration and amyotrophic lateral sclerosis.
Cytosolic aggregates of TDP-43 or FUS are common pathological hallmarks in these disorders.

Purpose of the Study:

To review the role of messenger ribonucleoprotein (mRNP) granules in the formation of RNA-binding protein aggregates.
To discuss how the dynamics of mRNP granules may be disrupted in neurodegenerative diseases.
To explore the contribution of these disruptions to neuronal dysfunction and neurotoxicity.

Main Methods:

Literature review focusing on the functional properties of mRNP granules.
Analysis of evidence linking mRNP granule dynamics to TDP-43 and FUS aggregation.
Discussion of in vitro and in vivo mechanisms of RBP aggregation within granules.

Main Results:

mRNP granules, such as stress and transport granules, can act as "catalytic convertors" for RBP aggregation.
High concentrations of RBPs, particularly those with low-complexity domains, can lead to granule "solidification" and loss of dynamic properties.
Disrupted granule dynamics contribute to altered stress responses, mRNA transport, local translation, and the formation of pathological TDP-43/FUS aggregates.

Conclusions:

Dynamic mRNP granules can transition into pathological aggregates containing misfolded RBPs like TDP-43 and FUS.
Abnormal interactions within RBP low-complexity domains drive granule solidification and dysfunction.
This process contributes to neurodegeneration by impairing neuronal functions and promoting RBP aggregation.