Role of surface condensation for the assembly of cortical proteins (A1)

The goal of A1 is to understand how surface condensation of scaffold proteins at biological membranes can control the patterning and the mechanics of an acto-myosin cell cortex.

The formation of epithelial tissue requires precise spatiotemporal control of cell surface properties such as formation of adhesion complexes that are linked to the cell cortex at the level of the cell membrane^1,2. The Honigmann group has discovered that surface condensation of ZO scaffold proteins at the membrane is a mechanism that cells exploit to pattern adhesion complexes and the actin cortex³. In vitro reconstitutions have shown that ZO surface condensates can nucleate and bundle actin fibers, which can drive the formation of a variety of cortical patterns^4-6. How ZO surface condensation and actin polymerization are linked and what mechanical properties emerge from this is not understood.

How does surface condensation of ZO proteins induce actin recruitment and polymerization? and What are the mechanical properties of a condensed ZO1-actin cortex on the membrane?

Linking surface condensation of scaffold proteins to the assembly of cell junctions

The PhD students will be trained in protein and membrane biochemistry methods including membrane reconstitutions, biophysical methods such as fluorescence fluctuation spectroscopy, in addition to super-resolution microscopy and image analysis methods.

• Candidates have a Masters degree in biophysics or related fields
• Candidates are expected to have a solid basis in physics, biology, or related fields.
• Experience in fluorescence microscopy is plus

We are currently recruiting the first cohort of motivated doctoral candidates to join our research training group “RTG 3120 Biomolecular Condensates”. If you are a potential applicant, register and complete the following form . If you have questions about the research topic, then email the project supervisor >