Recruiting Faculty

Dorothee Dormann's picture

Prof. Dr. Dorothee Dormann

Johannes Gutenberg University Mainz - Institute of Molecular Biology (IMB)
Neurodegeneration

Research Mission
Our research focuses on the molecular mechanisms of RNA-binding protein (RBP) dysfunction in neurodegenerative diseases, most notably the currently incurable disorders ALS (amyotrophic lateral sclerosis), FTD (frontotemporal dementia), and Alzheimer's disease. We aim to understand how specific, disease-linked RBPs, such as TDP-43 and FUS, mislocalize and aggregate in these disorders, to provide a mechanistic basis for new therapeutic strategies.

Experimental Techniques
We dissect the complex pathomechanism using a reductionist approach based on in vitro reconstitution and cellular experiments. We use recombinant proteins, protein/RNA biochemistry and biophysics to understand molecular events. As cellular models, we mostly use mammalian cell lines. We use techniques such as confocal microscopy, live cell imaging, protein-RNA interaction and phase separation assays, and employ genomics and proteomics approaches.

Selected Publications

Disease-linked TDP-43 hyperphosphorylation suppresses TDP-43 condensation and aggregation

EMBO Journal  2022


Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation

Cell 2018



Achilleas Frangakis's picture

Prof. Dr. Achilleas Frangakis

Goethe University Frankfurt - Institute of Biophysics
Bioimaging

Research Mission
Cell adhesion is an essential process that allows for cells to attach and interact with other cells and their environment in order to perform a multitude of tasks. Although adhesion is directly related to infection processes and disease, it is currently only poorly understood. Our mission is to study and decipher the adhesion mechanisms of both eukaryotic and bacterial cells.

Experimental Techniques
We use a large arsenal of different technologies to complement our primary methodologies of cryo-electron tomography, image processing and machine learning. Our main model system to study bacterial adhesion is M. pneumoniae & genitalium. For eukaryotic systems we utilise various endothelial and epithelial cell lines.

Ana García Sáez's picture

Prof. Dr. Ana García Sáez

MPI of Biophysics
Bioimaging

Research Mission
Our department aims at understanding the underlying physical principles and molecular mechanisms that govern membrane organization and dynamics. A key open question is how membrane behavior and signaling are coordinated by the interplay between molecular components and the membrane properties. We focus our research on the mitochondrial alterations during apoptosis as well as on membrane permeabilization as a common theme in regulated cell death.

Experimental Techniques
We have established a multi-disciplinary department that develops new microscopy tools and combines biophysics, biochemistry and cell biology in reconstituted minimal systems and in single cells to analyze mitochondrial permeabilization and additional alterations during apoptosis from a quantitative perspective. We also apply these methods to study the molecular mechanisms of membrane permeabilization that execute other forms of cell death.

Selected Publications

The interplay between BAX and BAK tunes apoptotic pore growth to control mitochondrial DNA-mediated inflammation

Molecular Cell 2022


DRP1 interacts directly with BAX to induce its activation and apoptosis

EMBO Journal 2022


BCL-2-family protein tBID can act as a BAX-like effector of apoptosis

EMBO Journal  2022



Bernhard Hampölz's picture

Dr. Bernhard Hampölz

MPI of Biophysics - Molecular Sociology
Cell Biology

Research Mission
Our aim is to better understand how macromolecular complexes and in particular the Nuclear Pore Complex (NPC) assemble in the context of animal development. To that end we use embryos and the female germline of the fruitfly Drosophila melanogaster to delineate principles of how NPCs form in a multicellular organism and how their assembly relies on the major regulatory inputs of early development.

Experimental Techniques
Our methodological repertoire is broad and spans techniques as diverse as cultivating and crossing fruitfly lines (aka “Fly pushing”) and in vitro biochemistry. This spectrum contains Drosophila genetics, general cell biological techniques, organ dissection, plastic and Cryo-EM (including CLEM). Our core technology is imaging of living Drosophila embryos, ovaries and larval brains.

Selected Publications

Nuclear Pores Assemble from Nucloporin Condensates During Oogenesis

Cell 2019


Pre-assembled Nuclear Pores Insert Into the Nuclear Envelope During Early Development

Cell 2016



Inga Hänelt's picture

Prof. Dr. Inga Hänelt

Goethe University Frankfurt - Institute of Biochemistry
Biochemistry

Research Mission
Proteins involved in substrate translocation across biological membranes are diverse and the variety that nature has evolved to control substrate flux absolutely fascinates us. A major focus of my group is on bacterial membrane transport systems and, in particular, potassium transport systems that are essential for the survival of a single cell and a bacterial community, namely biofilms.

Experimental Techniques
Our lab applies a variety of methods, including biochemistry, structural biology, EPR spectroscopy, microbiology and electrophysiology for understanding the molecular principles of membrane transport proteins.

Gerhard Hummer's picture

Prof. Dr. Gerhard Hummer

MPI of Biophysics - Theoretical Biophysics
Biophysics

Research Mission
We use molecular dynamics simulations and integrative modeling to study biological systems from molecular to organellar scales. Focus areas include the dynamics of the nuclear pore complex; membrane remodeling in cell homeostasis, autophagy and viral infection; and membrane channel and transporter function. To tackle issues of size and complexity in molecular dynamics simulations at organellar scales, we develop novel simulation and AI methods.

Experimental Techniques
We use a wide range of computational and theoretical techniques including molecular dynamics simulations; integrative modeling; artificial intelligence / machine learning; statistical physics; computational physics; theoretical chemistry; quantum chemistry; computational chemistry; bioinformatics; high-performance computation; kinetic modeling; stochastic processes; and Bayesian statistics.

Selected Publications

Artificial intelligence reveals nuclear pore complexity

bioRxiv 2022


Global structure of the intrinsically disordered protein tau emerges from its local structure

JACS Au 2022


Membrane fusion and drug delivery with carbon nanotube porins

Proc. Natl. Acad. Sci. U.S.A. 2021


FAM134B-RHD protein clustering drives spontaneous budding of asymmetric membranes

J. Phys. Chem. Lett. 2022


In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges

Science 2021



Edward A Lemke's picture

Prof. Dr. Edward A Lemke

Johannes Gutenberg University Mainz - Institute of Molecular Biology (IMB)
Biophysics

Research Mission
We focus on studying intrinsically disordered proteins (IDPs), which constitute up to 50% of the eukaryotic proteome. IDPs are found in many vital biological processes, such as nucleocytoplasmic transport, transcription and gene regulation. The ability of IDPs to exist in multiple conformations is considered a major driving force behind their enrichment during evolution in eukaryotes.

Experimental Techniques
Using a question-driven, multidisciplinary approach paired with novel tool development in miroscope engeenering, chemical biology, synthetic biology and microfludics, we have made major strides in understanding the biological dynamics of such systems from the single molecule to the super resolved whole cell level.

Selected Publications

Visualizing the disordered nuclear transport machinery in situ

Nature 2023



Melanie McDowell's picture

Dr. Melanie McDowell

MPI of Biophysics
Structural Biology

Research Mission
Almost all eukaryotic membrane proteins start their life in the cytosol and must journey to the cellular membrane where they function. Multiple pathways are employed to recognise different classes of membrane proteins, deliver them to the correct membrane and insert them into the lipid bilayer. We strive to understand the protein factors involved in these pathways at the endoplasmic reticulum, the primary destination for most membrane proteins.

Experimental Techniques
We use an integrative approach to study protein structure, interactions and function. Techniques include cryo-EM, x-ray crystallography, biophysical methods, in vitro biochemical reconstitution and pull-outs of native protein complexes from model organisms such as yeast and Chaetomium thermophilum.

Selected Publications

Structural and molecular mechanisms for membrane protein biogenesis by the Oxa1 superfamily

Nature Structural and Molecular Biology 2021


Structural basis of tail-anchored membrane protein biogenesis by the GET insertase complex

Molecular Cell 2020



Nina Morgner's picture

Prof. Dr. Nina Morgner

Goethe University Frankfurt - Institute of Physical and Theoretical Chemistry
Physical Chemistry

Research Mission
Cellular function is generally controlled by non-covalent interactions between proteins and other biomolecules. We investigate such interactions, molecular machines and their assembly by means of native mass spectrometry (MS). Where current technology is not sufficient to answer we further develop mass spectrometric instrumentation.

Experimental Techniques
Our research makes use of two different non-covalent MS methods. One is the commercially available nESI-MS method, the other LILBID MS, which we develop in house.

Selected Publications

Bacterial F-type ATP synthases follow a well-choreographed assembly pathway.

Nature communications 2022


LILBID laser dissociation curves: a mass spectrometry-based method for the quantitative assessment of dsDNA binding affinities.

Scientific reports 2020


Structural rearrangement of amyloid-β upon inhibitor binding suppresses formation of Alzheimer’s disease related oligomers

eLife 2020



Michaela Müller-McNicoll's picture

Prof. Dr. Michaela Müller-McNicoll

Goethe University Frankfurt - Institute for Molecular Bio Science
Gene Regulation

Research Mission
RNA binding proteins with low complexity domains (LCDs) often assemble nuclear compartments or large RNA-protein particles under stress. We study how RNA-protein interactions organize subcellular architecture and coordinate the regulation of gene expression during cellular stress and differentiation. Our goal is to understand how different steps in gene expression are interconnected in time and separated in space.

Experimental Techniques
Using pluripotent cells as a model system, we combine various methods including smRNA FISH, imaging, protein/RNA Biochemistry, iCLIP, Ribo-seq, metabolic labelling, reporter gene studies, mass spectrometry, CRISPR mutagenesis and RNA bioinformatics to obtain mechanistic insights. We also develop new methods and assays to get a quantitative and high-resolution picture of gene expression in the context of a compartmentalized cell.

Selected Publications

Poison exon splicing of SRSF6 regulates nuclear speckle dispersal and the response to hypoxia.

Nucleic Acids Research  2023


SRSF3 and SRSF7 affect 3’UTR length in opposite directions through suppression or activation of proximal poly(A)-sites and regulation of CFIm levels.

Genome Biology 2021


SRSF7 maintains its homeostasis through the expression of Split-ORFs and nuclear body assembly

Nature Structural Molecular Biology 2020


Cellular differentiation state modulates the export activity of SR proteins.

Journal of Cell Biology 2017


hGRAD: A versatile "one-fits-all" system to acutely deplete RNA binding proteins from condensates

Journal of Cell Biology 2024



Christian Münch's picture

Prof. Dr. Christian Münch

Goethe University Frankfurt - Institute of Biochemistry II (IBC2)
Cell Biology

Research Mission
Cells respond to stress with highly coordinated and dynamic responses. Their full complexity and spatio-temporal control remains poorly understood. We focus on a range of stresses - (mitochondrial) protein misfolding, infection, cancer - to study their effects on a systems biology/medicine level. We aim to define the molecular details of stress responses, their roles in diseases, and potential avenues for therapeutic intervention.

Experimental Techniques
We employ biochemical, cell biological, genetic, and proteomics approaches to comprehensively monitor the multiple facets of stress responses. To grasp dynamic, cell-wide changes, we develop proteomics methods, such as for translation & degradation. We then apply computational approaches on our multi-level data to gain integrated systems information. Our work largely focuses on mammalian cell culture systems and clinical models.

Selected Publications

A cytosolic surveillance mechanism activates the mitochondrial UPR

Nature 2023


Global mitochondrial protein import proteomics reveal distinct regulation by translation and translocation machinery

Molecular Cell 2022


Protein import motor complex reacts to mitochondrial misfolding by reducing protein import and activating mitophagy

Nature Commun 2022


Proteomics of SARS-CoV-2-infected host cells reveals therapy targets

Nature 2020


Functional Translatome Proteomics Reveal Converging and Dose-Dependent Regulation by mTORC1 and eIF2α

Molecular Cell 2020



Klaas Martinus Pos's picture

Prof. Dr. Klaas Martinus Pos

Goethe University Frankfurt - Institute of Biochemistry
Biochemistry

Research Mission
We look into the molecular detail of antibiotic efflux pump and lipid transport machineries and how these pumps can provide resistance against many antibiotics. We also research on efflux pump inhibitors, which can be used in combination with existing antibiotics to recover their effectiveness.

Experimental Techniques
We use X-ray crystallography and single-particle Cryo-EM to obtain molecular insight into the mechanisms of antibiotic binding and transport. With biophysical and biochemical methods, we quantify the effectiveness of the efflux pump inhibitors and gain insight into antibiotic interaction with the efflux pump

Selected Publications

Pyridylpiperazine efflux pump inhibitor boosts in vivo antibiotic efficacy against K. pneumoniae.

EMBO Mol Med 2024


Pyridylpiperazine-based allosteric inhibitors of RND-type multidrug efflux pumps

Nat Commun 2022


Allosteric drug transport mechanism of multidrug transporter AcrB

Nat Commun 2021



Beata Turoňová's picture

Dr. Beata Turoňová

MPI of Biophysics - Molecular Sociology
Structural Biology

Research Mission
We aim to facilitate in situ structural analysis by developing novel algorithms for cryo electron tomography and subtomogram averaging. Our method development focuses on improving tomogram quality and integrating contextual information into subtomogram averaging routines. The goal is to allow for reliable and objective analysis of tomograms as well as macromolecular complexes.

Experimental Techniques
The main focus is software method development. We use cryo electron tomography, often in combination with focused ion-beam milling, to obtain data for the method development. To ensure their robustness, the methods are tested on a variety of samples from virus-like particles (e.g. HIV, Sars-Cov-2) and real viruses (e.g. Sars-Cov-2, vaccinia) to very large macromolecular complexes (e.g. nuclear pore complexes).

Selected Publications

In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges

Science 2020


Benchmarking tomographic acquisition schemes for high-resolution structural biology

Nature Communications 2020


Cone-shaped HIV-1 capsids are transported through intact nuclear pores

Cell 2021



Janet Vonck's picture

Dr. Janet Vonck

MPI of Biophysics - Structural Biology
Structural Biology

Research Mission
Membrane proteins play essential roles in many cellular processes including transport, creating and maintaining ion gradients, and signaling, between cellular compartments and the cell and its environment. But our knowledge of their structure is still far behind that of soluble proteins. We study the structure and dynamics of membrane proteins and membrane protein complexes by cryo-EM.

Experimental Techniques
We use the pipeline of single-particle cryo-EM from sample vitrification, microscope data collection, image processing and particle reconstruction to model building.

Selected Publications

High-resolution structure and dynamics of mitochondrial complex I – insights into the proton pumping mechanism

Science Advances 7, eabj3221 2021


Structural basis of proton-coupled potassium transport in the KUP family

Nature Communications 11, 626 2020


Structure, mechanism, and regulation of the chloroplast ATP synthase

Science 360, eaat4318  2018



Florian Wilfling's picture

Dr. Florian Wilfling

MPI of Biophysics
Cell Biology

Research Mission
Proteins are workhorses of cells and perform a vast array of functions. Often this requires the formation of large multi-protein complexes which act as a macromolecular machine for individual tasks. How disused, damaged or misassembled macromolecular machines are disposed is largely unknown. Our main goal is to systematically identify signals and factors important for surveillance of the assembly and functional state of macromolecular machines.

Experimental Techniques
We integrate a diverse set of techniques including biochemistry, advanced live-cell microscopy, correlative cryo-electron tomography, state-of-the-art quantitative mass spectrometry and unbiased system-wide approaches.

Selected Publications

Selective autophagy degrades nuclear pore complexes

Nature Cell Biology 2020


A selective autophagy pathway for phase separated endocytic protein deposits

Molecular Cell 2020