Prof. Dr. Stefan Raunser

Stefan Raunser, geboren 1976 in Landau in der Pfalz, studierte von 1995 - 2000 Chemie und Biologie an der Johannes-Gutenberg-Universität Mainz. Er fertigte seine Doktorarbeit in der Arbeitsgruppe um Prof. Dr. Werner Kühlbrandt am Max-Planck-Institut für Biophysik in Frankfurt an und promovierte 2004 im Fach Biochemie an der Johann-Wolfgang-Goethe Universität Frankfurt.

Von 2005 bis 2008 war er Postdoktorand in der Arbeitsgruppe von Prof. Dr. Thomas Walz an der Harvard Medical School in Boston, USA. 2008 kehrte er nach Deutschland zurück und wurde Emmy-Noether-Gruppenleiter am Max-Planck-Institut für molekulare Physiologie in Dortmund. Von Januar bis Juni 2014 war er Einstein-Professor für Membranbiochemie an der Freien Universität Berlin.

Seit Juli 2014 ist er Direktor und Wissenschaftliches Mitglied am Max-Planck-Institut für molekulare Physiologie in Dortmund.

Im März 2015 wurde er Honorarprofessor an der Universität Duisburg-Essen und seit Mai 2015 ist er außerordentlicher Professor der Fakultät Chemie und Chemische Biologie der TU Dortmund.

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Vita

CompleteVita   

Education

2001 – 2004
PhD in Biochemistry, University of Frankfurt, Germany, Supervisor: Dr. Werner Kühlbrandt,
Max Planck Institute of Biophysics, Frankfurt, Germany

1995 – 2000
Diploma degree (equivalent to M.Sc.) in Biology, University of Mainz, Germany
First German State Examination in Chemistry and Biology, University of Mainz, Germany 
Supervisor of diploma thesis: Dr. H. Paulsen, University of Mainz, Germany

1995
Abitur with specialization in Biology, Chemistry and English

Current Positions

2015 – now
Honorary Professor, University of Duisburg-Essen, Germany

2015 – now
Adjunct Professor, Technical University Dortmund, Germany

2014 – now
Director, Department of Structural Biochemistry,
Max Planck Institute of Molecular Physiology, Dortmund, Germany

Previous Positions

2014
Full Professor, Department of Chemistry/Biology/Pharmacy,
Freie Universität Berlin, Germany

2008 – 2013
Independent Group Leader, Department of Physical Biochemistry,
 Max Planck Institute of Molecular Physiology, Dortmund, Germany

2005 –2008

Postdoctoral Researcher in the laboratory of Dr. T. Walz,
HHMI, Department of Cell Biology, Harvard Medical School, Boston, USA

Fellowships and Awards

2016
Randall Lecture – King’s College London University

2014
ERC Consolidator Grant

2013
Einstein-Professorship of the Einstein Foundation Berlin

2011 – 2014
Member of the “Junges Kolleg” (Academy of Sciences and Arts of North Rhine-Westphalia)

2009 – 2011
Member of the Global Young Faculty; Speaker of the Health group

2008 – 2013
Emmy-Noether Fellowship German Research Foundation (DFG)

2007 – 2008
Fellow of the German Academy of Sciences “Leopoldina”

2005 – 2006
Fellow of Harvard Medical School

2001 – 2004
Fellow of the German National Academic Foundation

1999
Fellow of the Johannes-Gutenberg University Foundation

1998 – 1999
Erasmus Fellow of the European Union

1995
Winner of the “Jugend forscht” competition in Palatinate


Ausgewählte Publikationen 2013-2019

 Publikationsliste 02/2020 

Gatsogiannis C, Balogh D, Merino F, Sieber SA, Raunser S (2019). Cryo-EM structure of the ClpXP protein degradation machinery. Nat Struct Mol Bio
doi: 10.1038/s41594-019-0304-0.

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
doi: 10.1038/s41467-019-11094-z.

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
doi: 10.1038/s41586-018-0556-6.

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
doi: 10.7554/eLife.36615.

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
doi: 10.7554/eLife.27434.

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
doi: 10.1073/pnas.1707506114

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.
doi: 10.1038/nature18295
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.
doi: 10.1038/nsmb.3281
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.
doi: 10.1016/j.str.2014.10.013

Efremov R, Hofnagel O, Raunser S (2015). Architecture and Conformational Switch Mechanism of the Ryanodine Receptor. Nature 517(7532):39-43.
doi: 10.1038/nature13916
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.
doi: 10.1016/j.cell.2015.09.027

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.
doi: 10.1038/nature14033
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.
doi: 10.1038/nature13015
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
doi: 10.1038/nature11987
freely available!

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