MSCA Doctoral Network PhD position: MS-based proteomic profiling of unmodified and modified β-cateni

11 ott - Roma
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Organisation/Company University of Milan Research Field Chemistry » Biochemistry Researcher Profile First Stage Researcher (R1) Positions PhD Positions Application Deadline 31 Oct 2026 - 23:59 (Europe/Vienna) Country Italy Type of Contract Temporary Job Status Full-time Hours Per Week 40 Offer Starting Date 1 Jan 2027 Is the job funded through the EU Research Framework Programme? Horizon Europe - MSCA Marie Curie Grant Agreement Number Is the Job related to staff position within a Research Infrastructure? Yes
Offer Description University of Milan
Project Title: MS-based proteomic profiling of unmodified and modified β-catenin- and β-catenin-peptide binder-sequences to decipher the role of protein PTMs in the IDR-mediated β-catenin interactome
Objectives:
1. Develop and benchmark quantitative MS-based proteomic strategies to resolve PTM-dependent β-catenin interaction networks, integrating affinity-based interactomics with perturbation-driven proteomic readouts.
2.



Define how individual and combinatorial PTMs—including S/T phosphorylation and R methylation—rewire β-catenin/IDR interaction networks and propagate into measurable cellular proteomic responses.
3. Establish quantitative proteomic signatures linking defined molecular perturbations of the β-catenin system to interaction-network remodeling and downstream pathway states, thereby distinguishing direct PTM-dependent interactions from secondary cellular responses.
Project Overview: Recent evidence shows that PRMT2 directly methylates β-catenin, promoting its proteasomal degradation and thereby attenuating downstream transcriptional activity. This places arginine methylation upstream in the regulation of β-catenin protein stability and provides a compelling mechanistic foundation for investigating β-catenin methylation and its crosstalk with phosphorylation. Building on these findings, this project will investigate how specific PTMs—and defined combinations of PTMs—encode different molecular and cellular states o

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