Stefan Raunser

Director, Structural Biochemistry

News and Press Releases

Breakthrough Discovery Sheds Light on Heart and Muscle Health

November 01, 2023

Scientists shoot first true-to-life 3D image of the thick filament of mammalian heart muscle more

Through the backdoor: How phosphate escapes from actin

MPI scientists reveal how phosphate escapes from actin filaments – a key signal that primes older filaments for disassembly more

BRAIN LOGISTICS: Missing link explains mRNA delivery in brain cells

June 01, 2023

Teams from MPI Institutes in Dresden, Dortmund, Frankfurt am Main and Göttingen have joined forces to gain the first evidence of a protein complex responsible for the transport of messenger RNA in neurons more

Novel AI-based software enables quick and reliable imaging of proteins in cells

May 15, 2023

Max Planck researchers from Dortmund programmed a tool that accurately recognises and picks proteins in electron cryo-tomography, substituting troublesome hand selection more

Research Interests

> Department Structural Biochemistry

Our research concentrates on the molecular understanding of fundamental cellular processes. Firstly, we are interested in membrane homeostasis in eukaryotic cells and secondly we want to understand the molecular details of muscle contraction. Another focus is on the molecular understanding of the mechanism of action of bacterial toxin complexes.
Our overarching goal is to understand the mechanisms underlying these processes in the healthy and diseased organism in molecular detail. To achieve this, it is essential to elucidate the structure and thus the function of the involved proteins and protein complexes.
We perform structural analyses by electron cryomicroscopy (cryo-EM) and electron cryotomography (cryo-ET), fluorescence-based assays and site-directed mutagenesis to determine the structures and functions of these complexes. For their biophysical characterization we employ isothermal titration calorimetry, ESI-MS, bio-layer interferometry, thermophoresis and CD spectroscopy.

The potential of cryo-electron tomography

We use single particle cryo-electron microscopy (cryo-EM) and cryo-electron tomography (cryo-ET) to study muscle contraction in health and disease. In particular, we apply cryo-ET to understand how muscle proteins work within their cellular environment, i.e. the myofibril. Watch this video to see why we feel that cryo-ET is the key structural biology technique of the future.

https://www.youtube.com/watch?v=nuyp6Q7jYEA

<p>Watch how an international Team led by Prof. Stefan Raunser has produced the first high-resolution 3D image of the sarcomere, the basic contractile unit of skeletal and heart muscle cells, by using electron cryo-tomography (cryo-ET).</p>

Zooming in on Muscle Cells

Watch how an international Team led by Prof. Stefan Raunser has produced the first high-resolution 3D image of the sarcomere, the basic contractile unit of skeletal and heart muscle cells, by using electron cryo-tomography (cryo-ET).

https://www.youtube.com/watch?v=5ViX-nsehsg

Bacteria have developed different strategies to infect organisms and use them as food sources. Bacteria such as the plague pathogen <em>Yersinia pestis</em> or bacteria from the <em>Salmonella</em> family use a complex toxin whose mode of action had not been investigated until recently. This video shows how the Tc toxin enters the host cell and kills it.<br />

Mechanism of Tc Toxin Action

Bacteria have developed different strategies to infect organisms and use them as food sources. Bacteria such as the plague pathogen Yersinia pestis or bacteria from the Salmonella family use a complex toxin whose mode of action had not been investigated until recently. This video shows how the Tc toxin enters the host cell and kills it.

https://www.youtube.com/watch?v=Y1dMsNyW5Zo

Selected Publications

PubMed List>

Tamborrini D, Wang Z, Wagner T, Tacke S, Stabrin S, Grange M, Kho AL, Rees M, Bennet P, Gautel M, Raunser S (2023). Structure of the native myosin filament in the relaxed cardiac sarcomere. Nature
Source

Rice G, Wagner T, Stabrin M, Sitsel O, Prumbaum D, Raunser S (2023). TomoTwin: generalized 3D localization of macromolecules in cryo-electron tomograms with structural data mining. Nature Methods
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Oosterheert W, Klink B. U, Belyy A, Pospich S, Raunser S (2022). Structural Basis of actin filament assembly and aging. Nature
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Wang Z, Grange M, Pospich S, Wagner T, Kho A.L, Gautel M, Raunser S (2022). Structures from intact myofibrils reveal mechanism of thin filament regulation through nebulin. Science
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Link to freely available Paper!

Wang Z, Grange M, Wagner T, Kho AL, Gautel M, Raunser S (2021). The molecular basis for sarcomere organization in vertebrate skeletal muscle. Cell
Source

Gatsogiannis C, Balogh D, Merino F, Sieber SA, Raunser S (2019). Cryo-EM structure of the ClpXP protein degradation machinery. Nat Struct Mol Bio
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Raisch T, Chang CT, Levdansky Y, Muthukumar S, Raunser S, Valkov E (2019). Reconstitution of recombinant human CCR4-NOT reveals molecular insights into regulated deadenylation. Nature Communications
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Gatsogiannis C, Merino F, Roderer D, Balchin D, Schubert E, Kuhlee A, Hayer-Hartl M, Raunser S. (2018). Tc toxin activation requires unfolding and refolding of a β-propeller. Nature
Source

Vinayagam D, Mager T, Apelbaum A, Bothe A, Merino F, Hofnagel O, Gatsogiannis C, Raunser S (2018). Electron cryo-microscopy structure of the canonical TRPC4 ion channel. eLife
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Klink BU, Zent E, Juneja P, Kuhlee A, Raunser S, Wittinghofer A. (2017). A recombinant BBSome core complex and how it interacts with ciliary cargo. eLife
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Pospich S, Kumpula EP, von der Ecken J, Vahokoski J, Kursula I, Raunser S. (2017). Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability. Proc Natl Acad Sci U S A
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von der Ecken J, Heissler SM, Pathan-Chhatbar S, Manstein DJ & Raunser S (2016).Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution. Nature 534(7609):724-28.
Source
freely available!

Gatsogiannis C, Merino F, Serdiuk T, Prumbaum D, Roderer D, Leidreiter F, Meusch D, Müller DJ, and Raunser S (2016). Membrane insertion of a Tc toxin in atomic detail. Nature Structural and Molecular Biology 23(10):884-890.
Source
freely available!

Gatsogiannis C, Hofnagel O, Markl J, Raunser S (2015). Structure of Mega-Hemocyanin reveals protein origami in snails. Structure 23(1):93-103.
Source

Efremov R, Hofnagel O, Raunser S (2015). Architecture and Conformational Switch Mechanism of the Ryanodine Receptor. Nature 517(7532):39-43.
Source
freely available!

Whitney JC, Quentin D, Sawai S, LeRoux M, Harding BN, Ledvina HE, Tran BQ, Robinson H, Goo YA, Goodlett DR, Raunser S, Mougous JD (2015). An Interbacterial NAD(P)(+) Glycohydrolase Toxin Requires Elongation Factor Tu for Delivery to Target Cells. Cell 163(3):607-19.
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von der Ecken J, Müller M, Lehman W, Manstein DJ, Penczek PA, Raunser S (2015). Structure of the F-actin-tropomyosin complex. Nature 519(7541):114-7.
Source
freely available!

Meusch D, Gatsogiannis C, Efremov R, Lang A, Hofnagel O, Vetter I, Aktories K, Raunser S (2014). Mechanism of Tc toxin action revealed in molecular detail. Nature 508(7494):61-5.
Source
freely available!

Gatsogiannis C, Lang A, Meusch D, Pfaumann V, Hofnagel O, Benz R, Aktories K, Raunser S (2013). A syringe-like injection mechanism in Photorhabdus luminescens toxins. Nature. 495(7442):520-23
Source
freely available!