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Regulation of membraneless organelles through phosphatase-DYRK kinase feedback

Project description

Dissecting the mechanism of physiological protein condensation: implications for neurodegenerative disorders

Neurodegeneration is associated with protein aggregates that lead to neuron atrophy and dysfunction. However, emerging evidence indicates that reversible condensates of proteins and RNAs may also have a physiological role in cells as non-membrane bound organelles. The scope of the EU-funded PhosphoMLO project is to identify how this process is regulated and determine how it becomes irreversible, leading to neurodegeneration. In this context, researchers will employ a multidisciplinary approach to identify regulators of protein condensation in Caenorhabditis elegans. The project has the potential to identify novel targets of therapeutic relevance for neurodegenerative diseases.

Objective

As the demographics of Europe and other developed countries shift ever older, neurodegenerative diseases involving aberrant protein aggregation grow more common but still lack effective treatment options. In healthy eukaryotic cells, the reversible weak aggregation of proteins and RNAs is necessary for the formation of condensates known as membraneless organelles. The roles of these condensates are still under investigation but may include concentrating proteins to facilitate reactions and buffering protein availability in a variety of cellular pathways. Identifying the molecular regulators of condensate assembly and maintenance is important to understand the transition from reversible to irreversible aggregation during disease and to determine potential therapeutic targets. The host lab has found that sufficient concentrations of the kinase DYRK3 trigger the dissolution of condensates, including splicing speckles, the pericentriolar matrix, and stress granules, by phosphorylating their component proteins. While in C. elegans, the serine/threonine phosphatase PP2A plays a crucial role in the assembly of membraneless organelles by dephosphorylating the substrates of the DYRK family kinase MBK-2, little is known about dephosphorylation of DYRK3 substrates in human cells or the regulation of DYRK3 activity. I hypothesize that feedback between DYRK3 and a phosphatase controls cycling of DYRK3 and its substrates between membraneless organelles and a dilute phase. I will apply interdisciplinary approaches including genetic perturbations, biochemical experiments, imaging, and mathematical modelling to address this hypothesis, in the process uncovering key regulators of condensate formation, emergent properties of feedback regulation, and a new mechanism for the regulation of phase-separated compartments.

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MSCA-IF - Marie Skłodowska-Curie Individual Fellowships (IF)

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(opens in new window) H2020-MSCA-IF-2020

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Coordinator

UNIVERSITAT ZURICH
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.

€ 191 149,44
Address
RAMISTRASSE 71
8006 Zurich
Switzerland

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Region
Schweiz/Suisse/Svizzera Zürich Zürich
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.

€ 191 149,44
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