PhD and Postdoc opportunities in the Netherlands

Interested in doing a PhD or a Postdoc in the Netherlands, or know someone who might? There are 20 vacancies available across five universities in the Netherlands. Please share this post with your networks of students and early-career researchers. The application deadline is 28 June 2024.
PhD and Postdoc opportunities in the Netherlands
Like

Share this post

Choose a social network to share with, or copy the shortened URL to share elsewhere

This is a representation of how your post may appear on social media. The actual post will vary between social networks

The 23M Euros Zwaartekracht research consortium FLOW – Protein Quality for Health aims to uncover completely the molecular principles of how the intrinsic cellular protein quality-control network modulates the trajectory of two human disease proteins, CFTR (loss of function) and a-synuclein (gain of toxicity), from cradle to grave. To meet this goal, the FLOW consortium – a unique, diverse, and highly interdisciplinary team – will combine biochemical, biophysical, cell biological, computational, and genetic methods, from computation and single molecule to cell. As part of the project, we are currently offering 20 PhD and Postdoc positions across five universities in the Netherlands.

The project FLOW is designed as three heavily interconnected work packages. While some projects put more emphasis on a specific work package, we expect all applicants to contribute to all of them and to both CFTR and α-synuclein. In FLOW WP 1 “Discover” we will establish all fates and interactors of both clients and the interactor’s effects on clients fates and on cells. FLOW WP 2 “Rebuild” zooms in on the molecular details of client triage by the Quality Control (QC) system through reconstitution of network nodes. In FLOW WP 3 “Control”, we will then integrate this knowledge to control the QC network towards health.

Discover (WP1) will determine the fates of a-Synuclein and CFTR in cells, identify their interaction partners with spatio-temporal resolution and establish the effect of client and QC-factor variation on the cell.

We will Rebuild (WP2) triaging for folding vs aggregation vs degradation in vitro, to understand decision making towards each fate. We will use WP1 & 2 results to develop a predictive model for triaging of protein-misfolding diseases.

Our overall goal is to obtain full Control (WP3) over the fate of all proteins and thereby over  health of cells.

The FLOW consortium is led by group leaders Ineke Braakman (Utrecht), and furthermore includes Stefan Rüdiger, Arnold Boersma, Peter van der Sluijs, Friedrich Foerster (Utrecht), Mireille Claessens (Twente), Mark Hipp, Kasia Tych, Harrie Kampinga (Groningen), Alfred Vertegaal, Monique Mulder, Anne Wentink (Leiden), and Martijn Huynen, Evan Spruijt (Nijmegen).

It is a collaboration between 12 research groups from these universities and university medical centers in The Netherlands:

  • Utrecht University
  • University of Twente, Enschede
  • UMCG, Groningen
  • LUMC, Leiden
  • RadboudUMC, Nijmegen
  • Radboud University, Nijmegen
  • University of Groningen
  • Leiden University

List of FLOW projects open for application

Scroll through the list of available research questions below and, if you are interested in any of them, find more information here.

Mapping the proteostasis landscape for CFTR

  • Principal Investigators: Ineke Braakman and Peter van der Sluijs
  • Key collaborations: Alfred Vertegaal, Mark Hipp, Arnold Boersma, Friedrich Förster, Harm Kampinga

Main research question
What are the fates of CFTR (the Cystic Fibrosis Transmembrane conductance Regulator) in cell systems and how do these fates change upon altering the proteostasis network?

Insights into the biochemistry and thermodynamics of protein aggregate management

  • Principal Investigator: Mireille Claessens
  • Key collaborations: Stefan Rüdiger, Evan Spruijt, Anne Wentink, Arnold Boersma

Main research question
How does the protein quality control system target and manage protein aggregates  with different biochemical and thermodynamic properties?

Imaging CFTR and a-synuclein biogenesis in situ

  • Principal Investigator: Friedrich Förster
  • Key collaborations: Ineke Braakman, Alfred Vertegaal, Peter van der Sluijs, Mark Hipp, Martijn Huynen

Main research question
Which interactors trigger distinct fates of CTFR and a-synuclein in the cell and how?

Mapping the proteostasis landscape for alpha-synuclein

  • Principal Investigator: Mark Hipp
  • Key collaborations: Alfred Vertegaal, Arnold Boersma, Ineke Braakman, Friedrich Foerster, Harm Kampinga, Peter van der Sluijs

Main research question
Define the potential fates of mutant and wildtype alpha-synuclein in cellular systems, and change it by altering the proteostasis network.

Decision-making on the fate of damaged proteins

  • Principal Investigator: Stefan Rüdiger
  • Key collaborations: Mireille Claessens, Kasia Tych, Anne Wentink (project 1);
    Mireille Claessens, Alfred Vertegaal, Monique Mulder, Friedrich Förster (project 2)

Main research questions
1. How do molecular chaperones control the fate of damaged proteins?
2. How do shape and properties of protein aggregates determine their fate?

Ubiquitin-proteasome mediated degradation of misfolded proteins

  • Principal Investigator: Alfred Vertegaal
  • Key collaborations: Ineke Braakman, Mark Hipp, Friedrich Foerster, Monique Mulder, Martijn Huynen, Peter van der Sluijs

Main research questions
How does the ubiquitin-proteasome system control the fate of damaged proteins to prevent protein aggregation?

Sensors to investigate chaperone-client interactions in cells and in vitro compartments

  • Principal Investigator: Arnold Boersma
  • Key collaborations: Anne Wentink, Alfred Vertegaal, Mark Hipp

Main research question
Can we design sensors that measure which chaperones interact when and where with their clients in cells? Can we also use these for high-throughput screening in vitro?

Explaining the origin of chaperone system complexity using systems biology

  • Principal Investigator: Martijn Huynen
  • Key collaborations: Evan Spruit, Harm Kampinga, Mark Hipp, Alfred Vertegaal

Main research question
Why are there, in human, so many different copies of the chaperone system proteins, and what determines their specificity for their clients?

Balancing protein degradation to prevent toxic aggregate accumulation

  • Principal Investigator: Monique Mulder
  • Key collaborations: Alfred Vertegaal, Stefan Rüdiger, Mark Hipp

Main research question
How does the ubiquitin-proteasome system orchestrate the fate of damaged proteins to avert protein aggregation?

Protein aggregation and chaperone activity in biomolecular condensates

  • Principal Investigator: Evan Spruijt
  • Key collaborations: Mireille Claessens, Stefan Rüdiger, Arnold Boersma, Sonja Schmid

Main research question
How does the local environment created by LLPS affect the triage of damaged or aggregation-prone proteins, and the downstream pathways?

Unravelling chaperone function on the single-molecule level

  • Principal Investigator: Kasia Tych
  • Key collaborations: Mireille Claessens, Stefan Rüdiger, Anne Wentink

Main research question
How do chaperones control the fate of damaged proteins?

Chaperones: cooperation to tackle aggregation

  • Principal Investigator: Anne Wentink
  • Key collaborations: Arnold Boersma, Mireille Claessens, Stefan Rüdiger

Main research question
How do chaperones prevent and reverse pathological protein aggregation?

Apply

Information on applying to these vacancies can be found on the project websiteApplication deadline is 28 June 2024. The sarting date, in consultation, will be from 1 September 2024.

Contact details

Project manager: Ilse Pool at [email protected]


Photo by jennieramida on Unsplash

Join the FEBS Network today

Joining the FEBS Network’s molecular life sciences community enables you to access special content on the site, present your profile, 'follow' contributors, 'comment' on and 'like' content, post your own content, and set up a tailored email digest for updates.