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Deciphering the regulatory logic of the ubiquitin system

Project description

Specificity for protein degradation in the ubiquitin system

Selective protein degradation via the ubiquitin-proteasome system (UPS) plays an important role in many cellular processes. The principal specificity determinants are E3 ubiquitin ligases, which recognise cognate degron motifs found in substrate proteins. However, for the majority of E3 ligases encoded in the human genome, little is known about how they recognise their substrates. Using an expression screening platform to perform proteome-wide stability profiling, the ERC-funded E3-SUBSTRATES project aims to address this bottleneck. It will first systematically interrogate the proteome to identify relevant E3 ligase substrates, followed by detailed mechanistic investigation of their mode of degradation. The findings on how specificity is attained in the UPS could open the door to future development of small molecule therapies.

Objective

As the primary route through which eukaryotic cells achieve selective protein degradation, the ubiquitin-proteasome system (UPS) plays a key role in virtually all critical cellular processes. A major unresolved question concerns how the ubiquitin system attains such high selectivity towards its myriad of substrates. The main specificity determinants are the E3 ubiquitin ligases, which recognise cognate ‘degron’ motifs found in substrate proteins. However, for the majority of the ~600 E3 ligases encoded in the human genome we still have little or no knowledge as to their substrates, and our understanding of degron motifs remains limited. This knowledge gap prevents us from appreciating how key cellular processes are regulated and impedes the development of small molecules capable of either inhibiting or hijacking E3 ligases for therapeutic benefit.

To complement the biochemical and proteomic techniques that have served as the primary route to discovery in the field, we seek to exploit functional genetic approaches to understand how E3 ligases recognise their substrates. Leveraging an expression screening platform that enables proteome-wide stability profiling, our specific goals are to: (1) identify physiological substrates regulated via degrons lying at their extreme C-termini, (2) define novel mechanisms through which conditional protein degradation is achieved via phospho-degrons, and (3) characterise the spectrum of degradative pathways responsible for the instability of hundreds of the most short-lived cellular proteins. For each goal, we will first provide global insight by systematically interrogating the proteome for relevant substrates; for the most interesting candidates, we will then seek detailed mechanistic understanding to illuminate new biology. Successful completion of this work will transform our understanding of how specificity is achieved within the UPS and greatly facilitate its future therapeutic manipulation.

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(opens in new window) ERC-2024-STG

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Host institution

THE CHANCELLOR MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE
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.

€ 1 528 843,00
Address
TRINITY LANE THE OLD SCHOOLS
CB2 1TN CAMBRIDGE
United Kingdom

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Region
East of England East Anglia Cambridgeshire CC
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.

€ 1 528 843,00

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