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Tuning TDP-43 self-assembly to understand physiological function and dysfunction

Project description

Untangling the dysfunction of RNA-binding proteins in disease

RNA-binding proteins are essential for gene expression, recognising hundreds of transcripts and forming extensive regulatory networks. Their dysfunction is linked to many diseases, including neurodegenerative disorders. The ERC-funded TDP-Assembly project will focus on molecular mechanisms that drive the dysfunction of the RNA-binding protein TDP-43, which underlies several neurodegenerative diseases. Specifically, TDP-43 may exhibit an aberrant self-assembly process that can lead to disturbed RNA processing. TDP-Assembly will use molecular and synthetic biology approaches to manipulate TDP-43 self-assembly in cells and study how this affects essential TDP-43 functions. Mapping various self-assembly processes and functions could shed light on the role of aberrant self-assembly in neurodegenerative disease.

Objective

Neurodegenerative disorders are an enormous societal burden and we lack therapies that target these diseases at their origins. To develop therapies, we need to understand what goes wrong at the molecular level. I uncovered key mechanisms that cause RNA-binding proteins, such as TDP-43, to dysfunction and drive neurodegenerative processes. I discovered that RNA-binding proteins self-assemble into ribonucleoprotein granules that are the likely origins of RNA-binding protein aggregates. More recently, my group and I revealed aberrant phase transitions of condensed RNA-binding proteins occurring in disease and identified fundamental mechanisms by which such phase transitions are regulated in cells.
In TDP-Assembly, I now want to find out why these proteins exhibit a self-assembly behavior that apparently risks pathological aggregation. My hypothesis is that self-assembly is essential for their many functions in gene regulation, and that different types of self-assemblies, e.g. small clusters or fluid or solid condensates, mediate different functions in cells. Using TDP-43 as a paradigm, I will test this hypothesis to ultimately understand the molecular basis of RNA-binding protein dysfunction in neurodegeneration.
To achieve this goal, I will use synthetic biology approaches to rationally tune self-assembly of TDP-43 in cells. I will study how altered TDP-43 self-assembly affects its known molecular functions, i.e. regulation of transcription, alternative splicing, and translation. Transcriptome and proteome analyses will draw a systems biology map of altered TDP-43 self-assembly and might lead us to novel functions of TDP-43 self-assembly. Ultimately, I will address how TDP-43's self-assembly, and thus its functions, are altered by disease-linked mutations in neuronal cells.
TDP-Assembly will forge a new understanding of the functional and pathological relevance of RNA-binding protein self-assembly and might inspire new therapies that target self-assembly processes.

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HORIZON-ERC - HORIZON ERC Grants

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Call for proposal

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(opens in new window) ERC-2023-COG

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Host institution

JOHANNES GUTENBERG-UNIVERSITAT MAINZ
Net EU contribution

Net EU financial contribution. The sum of money that the participant receives, deducted by the EU contribution to its linked third party. It considers the distribution of the EU financial contribution between direct beneficiaries of the project and other types of participants, like third-party participants.

€ 1 919 989,00
Address
SAARSTRASSE 21
55122 MAINZ
Germany

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Region
Rheinland-Pfalz Rheinhessen-Pfalz Mainz, Kreisfreie Stadt
Activity type
Higher or Secondary Education Establishments
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Total cost

The total costs incurred by this organisation to participate in the project, including direct and indirect costs. This amount is a subset of the overall project budget.

€ 1 999 989,00

Beneficiaries (2)

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