Deciphering the molecular grammar of β-catenin/IDR interactions

Offer Description

Medical University of Graz

Project Title: Deciphering the molecular grammar of β-catenin/IDR interactions

Objectives:

1. Characterize interaction and structure of IDRs that interact with β-catenin and how this interaction is regulated by IDR/β-catenin phosphorylation.
2. Reveal how β-catenin regulates IDR-mediated condensate formation and function.

Project Overview: This project aims to decipher the general mechanisms of β-catenin/IDR interactions. For example, IDRs of transcription factors (TFs) or scaffold proteins play critical roles in transcriptional regulation by recruiting co-factors to specific sites. In particular, the role of β-catenin as transcriptional coactivator, aside from Wnt/β-catenin signaling, remains enigmatic. This is mostly because, despite their high abundance, β-catenin binding sites within IDRs are only poorly conserved in sequence, which complicates identification of novel β-catenin targets based on sequence comparison. This project builds on expertise in NMR-based structural biology and cell biology in the Madl group at MUG and requires expertise in high-throughput screening (Maric group), post-translational modification of IDRs (Conibear group), X-ray crystallography (Grossmann group) and mass spectrometry (Bonaldi group) to fully decipher the molecular requirements, details, and functional consequences of β-catenin binding to IDRs. The innovation in this project is the ability to unravel the ‘molecular grammar’ of β-catenin/IDR interactions, their regulation by PTMs, and the functional consequences, which is strongly facilitated in this doctoral network. The new molecular and mechanistic insights have the potential to uncover new sequences and binding sites for discovery and therapeutic development of specific β-catenin inhibitors. Contribution to the overall research program: Consolidating insights from synthesis and structural biology studies within FlexCAT to build a broad understanding of how β-catenin interacts with IDRs.

Skills and research profile: We seek a highly motivated candidate with a strong background in biochemistry, molecular biology, biophysics, structural biology, or a related field and a keen interest in intrinsically disordered proteins, protein-protein interactions, and transcriptional regulation. Experience in recombinant protein expression and purification, biochemical/biophysical characterization of protein interactions, and/or cell biology is highly desirable. Prior experience with NMR spectroscopy or other structural biology methods is advantageous but not essential. The candidate should be interested in combining NMR-based structural biology with quantitative interaction studies, biomolecular condensate assays, and complementary approaches including high-throughput screening, protein post-translational modification, X-ray crystallography, and mass spectrometry. Strong analytical skills, enthusiasm for interdisciplinary and collaborative research, and willingness to undertake international secondments within the FlexCAT network are expected.

Salary: The position is funded by the Horizon Europe MSCA-DN project FlexCAT (Grant Agreement No. 101311592) for three years. The selected candidate will be offered a competitive salary comprising a Living Allowance (adjusted by the country correction coefficient), a Mobility Allowance, and, if applicable, a Family Allowance. All allowances are subject to applicable social security contributions and taxation. Subject to availability, additional funding may be provided by the host institution and/or the supervising PI to support employment for a fourth year, where required or beneficial for completion of the doctoral programme.

Planned secondment: 1. Host: TUW; Supervisor: Dr. Anne Conibear; Length: 4 months. Purpose: Synthesis of PTM-IDRs.

Enrolment in Doctoral degree(s): International PhD Program BioMolStruct at MUG (Madl)

How to apply:
Applications are exclusively accepted through the Recruitment Portal (https://phdrecruiting.medunigraz.at/). The required information is specified in the recruitment portal and comprises:
• Motivation statement for selected DC projects
• Detailed CV; publication list if applicable
• BSc/MSc diplomas and academic transcripts/supplements
• Contact details for two referees

Applications will be assessed for eligibility and scientific/academic quality. Shortlisted applicants will be invited to interview. The final selection will follow the open, transparent and merit-based recruitment principles of MSCA.

Key dates:
• Applications open: 15 September 2026
• Applications close: 31 October 2026
• Online pre-interviews: early November 2026
• Final interviews: late November/early December 2026
• Decisions and offers: mid-December 2026
• Start: January 2027 – March 2027

Data protection statement
The personal data you provide as part of your application will be processed for the purposes necessary to administer the recruitment and selection process for the Doctoral Candidate position(s) for which you apply within the FlexCAT Marie Skłodowska-Curie Doctoral Network (MSCA-DN). Access to your application will be restricted to individuals directly involved in the recruitment and selection process, including the recruiting beneficiary, members of the selection committee, and, where necessary, authorised representatives of the FlexCAT consortium. Personal data will be processed in accordance with the applicable data-protection legislation, including the General Data Protection Regulation (EU) 2016/679 (GDPR), and the privacy policies of the recruiting beneficiary. Statistics for project reporting will be provided in anonymised or appropriately aggregated form.

Where to apply

Website: https://phd-recruiting.medunigraz.at/

Requirements

• Research Field: Chemistry
• Education Level: Master Degree or equivalent

Skills/Qualifications

General criteria:
Applicants of any nationality are welcome to apply. To be eligible for recruitment as an MSCA Doctoral Candidate, applicants must fulfil the following criteria at the date of recruitment:
• Education – you do not hold a doctoral degree and hold (or will shortly complete) a science Master’s degree (see individual project requirements), with excellent results, qualifying you for admission to the doctoral program of the respective host institution. The successful candidate must fulfil the admission requirements of the respective doctoral programme and will be enrolled in a doctoral programme during the project.
• Mobility - you must not have resided or carried out your main activity (work, studies, etc.) in recruiting beneficiary’s country for more than 12 months during the 36 months before your recruitment. Compulsory national service, holidays/short stays and time spent obtaining refugee status under the Geneva Convention4 are not considered for this purpose.
• Language & communication – excellent command of spoken and written English (min. B2 level). Ability to communicate results clearly to diverse audiences, both in writing and verbally.
• Motivation – motivation for multidisciplinary, international doctoral research, hands-on experimental work, mandatory academic/industy secondment(s), to publish research findings in international journals, present results at conferences and contribute to project deliverables. Willingness to contribute to project network-wide activities, communication, training events, and dissemination efforts.
• Technical skills – specific to the individual DC project (see individual project descriptions).

Specific Requirements

Skills and research profile: We seek a highly motivated candidate with a strong background in biochemistry, molecular biology, biophysics, structural biology, or a related field and a keen interest in intrinsically disordered proteins, protein-protein interactions, and transcriptional regulation. Experience in recombinant protein expression and purification, biochemical/biophysical characterization of protein interactions, and/or cell biology is highly desirable. Prior experience with NMR spectroscopy or other structural biology methods is advantageous but not essential. The candidate should be interested in combining NMR-based structural biology with quantitative interaction studies, biomolecular condensate assays, and complementary approaches including high-throughput screening, protein post-translational modification, X-ray crystallography, and mass spectrometry. Strong analytical skills, enthusiasm for interdisciplinary and collaborative research, and willingness to undertake international secondments within the FlexCAT network are expected.

• Languages: ENGLISH
• Level: Excellent
• Research Field: Chemistry
• Years of Research Experience: 1 - 4

Additional Information

Selection process

Applications will be assessed for eligibility and scientific/academic quality. Shortlisted applicants will be invited to interview. The final selection will follow the open, transparent and merit-based recruitment principles of MSCA.

Work Location(s)

• Number of offers available: 1
• Company/Institute: Medical University of Graz
• Country: Austria
• City: Graz

Contact

• City: Graz
• Website: https://phd-recruiting.medunigraz.at/