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Vorlage:Importartikel/Wartung-2023-11

Vorlage:Short description Vorlage:Orphan

Vorlage:Infobox scientist

Stefan Raunser[1] (born 1976[2] in Landau in der Pfalz, Germany) is a German scientist and structural biologist specializing in membrane proteins, the cytoskeleton, toxins, and sarcomere structural biochemistry. Since 2014, he has been a director at the Max Planck Institute of Molecular Physiology[3] in Dortmund, Germany.

Education and career[Bearbeiten | Quelltext bearbeiten]

Raunser studied biology and chemistry at the Johannes Gutenberg-Universität Mainz and completed his Ph.D. in biochemistry at the Goethe University Frankfurt in 2004, under the supervision of Prof. Werner Kühlbrandt at the Max Planck Institute of Biophysics in Frankfurt/Main.[4]

He continued his research as a postdoctoral researcher at Harvard Medical School in Boston, USA, working with Thomas Walz[5] from 2005 to 2008. He then became an "Emmy Noether group leader"[6] at the Max Planck Institute of Molecular Physiology in Dortmund, serving in that position from 2008 to 2013.[7] In 2014, Raunser held the Einstein Professorship[8] for Membrane Biochemistry at Free University of Berlin from January to June before assuming his current role as a director at the Max Planck Institute of Molecular Physiology.[9] In 2015, he became an honorary professor at the University of Duisburg-Essen,[10] and later that same year, he became an adjunct professor at Technical University of Dortmund.[11]

Research and selected publications[Bearbeiten | Quelltext bearbeiten]

The Raunser lab specializes in structural biochemistry, they employ and develop methods in CryoEM and CryoET to conduct research and uncover the molecular mechanisms in different aspects of cell biology.

Tc toxin complexes[Bearbeiten | Quelltext bearbeiten]

In the field of Tc toxins, tripartite ABC-type toxins from Photorhabdus luminescens and other bacteria that are used by the bacteria as virulence factors,[12] his research has focused on molecular mechanisms involved in toxin activation,[13] toxin release,[14] receptor binding,[15][16] membrane permeation,[17] protein translocation,[18][19] and intoxication.[20] His group published a movie of the intoxication process.[21] His work on Tc toxins has revealed their potential as customisable molecular syringes for delivering proteins across membranes, opening up possibilities for biotechnological and biomedical applications.[22][23]

Software and hardware development in cryoEM/cryoET[Bearbeiten | Quelltext bearbeiten]

The Raunser lab has contributed to developments in cryoEM image processing and cryoET hardware development.[24] They developed SPHIRE[25] (together with Pawel Penczek), which evolved later into TranSPHIRE.[26] The program offers an easy-to-use and versatile image processing suite for the single particle analysis of protein complexes in CryoEM. The group has also developed other software tools, such as SPHIRE-crYOLO[27] and TomoTwin,[28][29] for automatic particle picking in cryoEM and cryoET. On the CryoET front, the group has developed a streamlined workflow for automated cryo-focused ion beam milling for the analysis of vitrified samples by electron cryo tomography.[30]

Structural biochemistry of the cytoskeleton and muscle contraction[Bearbeiten | Quelltext bearbeiten]

Single particle approach[Bearbeiten | Quelltext bearbeiten]

Raunser's group has increased the resolution limits of single particle cryoEM reconstructions of muscle and cytoskeletal proteins, including actin filaments (F-actin),[31][32] actin filaments in complex with actin-binding proteins,[33] toxins[34][35] and ligands,[36][37] the actin-tropomyosin complex,[38] and the actomyosin complex.[39][40][41] The lab has determined the cryoEM structures of F-actin at ~2.2 Å resolution, allowing for the first time the direct visualisation of water molecules in the structure and giving atomic insight into ATP hydrolysis in F-actin[42][43][44][45] and phosphate release from the filament after hydrolysis.[46]

Tomography approach[Bearbeiten | Quelltext bearbeiten]

Raunser's group has revealed the three-dimensional organization of the sarcomere in situ,[47][48] resolving the molecular organization of myosin, alpha-actinin-1, and additional sarcomeric components. The group also determined the first structure of native nebulin bound to actin thin filaments within intact sarcomeres at 4.5 Å resolution,[49] and has successfully obtained the world's first high-resolution 3D image of the myosin thick filament in its natural cellular environment.[50][51]

Structural biochemistry of membrane proteins[Bearbeiten | Quelltext bearbeiten]

Raunser's group has made significant contributions to understanding the structures of key proteins involved in cell signaling, such as the rabbit ryanodine receptor 1[52] and the TRPC4 channel,[53] as well as the Drosophila's Slowpoke (Slo) potassium channel.[54] This research has provided insights into the regulatory mechanisms and revealed potential target sites for drug development.

Fellowships and awards (selection)[Bearbeiten | Quelltext bearbeiten]

References[Bearbeiten | Quelltext bearbeiten]

Vorlage:Reflist

External links[Bearbeiten | Quelltext bearbeiten]

{{Authority control}} {{DEFAULTSORT:Raunser, Stefan}} [[Category:1976 births]] [[Category:Living people]] [[Category:German biochemists]] [[Category:Max Planck Institute directors]] [[Category:European Research Council grantees]] [[Category:21st-century German biologists]] [[Category:Harvard Medical School alumni]] [[Category:Johannes Gutenberg University Mainz alumni]] [[Category:Goethe University Frankfurt alumni]] [[Category:Science teachers]] [[Category:European Molecular Biology Organization]] [[Category:Members of the German National Academy of Sciences Leopoldina]] [[Category:Structural biologists]] [[Category:German biologists]] [[Category:Max Planck Society people]] [[Category:People from Rhineland-Palatinate]]

  1. ↑ Stefan Raunser Orcid.
  2. ↑ Stefan Raunser Max Planck Institute.
  3. ↑ Raunser.
  4. ↑ Website of the Max Planck Institute of Molecular Physiology.
  5. ↑ Thomas Walz Lab HHMI page.
  6. ↑ Emmy Noether Programme. In: www.dfg.de. Abgerufen am 3. August 2023 (englisch).
  7. ↑ a b DFG - GEPRIS - Molecular regulation of cholesterol concentration in cell membranes. In: gepris.dfg.de. Abgerufen am 3. August 2023.
  8. ↑ a b Einstein Foundation Professorship - Stefan Raunser.
  9. ↑ Max Planck Institute Dortmund - Director Stefan Raunser.
  10. ↑ University of Duisburg-Essen - Honorary Professor Stefan Raunser.
  11. ↑ TU Dortmund - Professor Stefan Raunser.
  12. ↑ Daniel Roderer, Stefan Raunser: Tc Toxin Complexes: Assembly, Membrane Permeation, and Protein Translocation. In: Annual Review of Microbiology. 73. Jahrgang, Nr. 1, 8. September 2019, ISSN 0066-4227, S. 247–265, doi:10.1146/annurev-micro-102215-095531, PMID 31140906 (englisch, annualreviews.org).
  13. ↑ Max Planck Society: Researchers decode the toxin complex of the plague bacterium and other germs. In: phys.org. Abgerufen am 11. November 2023 (englisch).
  14. ↑ Oleg Sitsel, Zhexin Wang, Petra Janning, Lara Kroczek, Thorsten Wagner, Stefan Raunser: preprint article on bioRxiv. 2023, doi:10.1101/2023.02.22.529496 (doi.org).
  15. ↑ Daniel Roderer, Felix Bröcker, Oleg Sitsel, Paulina Kaplonek, Franziska Leidreiter, Peter H. Seeberger, Stefan Raunser: Glycan-dependent cell adhesion mechanism of Tc toxins. In: Nature Communications. 11. Jahrgang, Nr. 1. Springer Science and Business Media LLC, 2020, ISSN 2041-1723, S. 2694, doi:10.1038/s41467-020-16536-7, PMID 32483155, PMC 7264150 (freier Volltext), bibcode:2020NatCo..11.2694R.
  16. ↑ Ying Xu, Raghuvir Viswanatha, Oleg Sitsel, Daniel Roderer, Haifang Zhao, Christopher Ashwood, Cecilia Voelcker, Songhai Tian, Stefan Raunser, Norbert Perrimon, Min Dong: CRISPR screens in Drosophila cells identify Vsg as a Tc toxin receptor. In: Nature. 610. Jahrgang, Nr. 7931, Oktober 2022, ISSN 1476-4687, S. 349–355, doi:10.1038/s41586-022-05250-7, PMID 36171290, PMC 9631961 (freier Volltext), bibcode:2022Natur.610..349X (englisch).
  17. ↑ Christos Gatsogiannis, Felipe Merino, Daniel Prumbaum, Daniel Roderer, Franziska Leidreiter, Dominic Meusch, Stefan Raunser: Membrane insertion of a Tc toxin in near-atomic detail. In: Nature Structural & Molecular Biology. 23. Jahrgang, Nr. 10, Oktober 2016, ISSN 1545-9985, S. 884–890, doi:10.1038/nsmb.3281, PMID 27571177 (englisch, nature.com).
  18. ↑ Dominic Meusch, Christos Gatsogiannis, Rouslan G. Efremov, Alexander E. Lang, Oliver Hofnagel, Ingrid R. Vetter, Klaus Aktories, Stefan Raunser: Mechanism of Tc toxin action revealed in molecular detail. In: Nature. 508. Jahrgang, Nr. 7494. Springer Science and Business Media LLC, 23. Februar 2014, ISSN 0028-0836, S. 61–65, doi:10.1038/nature13015, PMID 24572368, bibcode:2014Natur.508...61M.
  19. ↑ Max Planck Society: Bacteria with vuvuzelas: Microbes use a channel protein as a syringe for toxins. In: phys.org. Abgerufen am 11. November 2023 (englisch).
  20. ↑ Mechanism of bacterial toxins in deadly attacks. In: EurekAlert! Abgerufen am 14. Oktober 2023 (englisch).
  21. ↑ Vorlage:Citation
  22. ↑ Max Planck Society: Protein injections in medicine. In: phys.org. Abgerufen am 11. November 2023 (englisch).
  23. ↑ Protein injections in medicine could one day be possible, says new study. In: Drug Target Review. Abgerufen am 11. November 2023 (englisch).
  24. ↑ ThermoFisher - lab portrait.
  25. ↑ SPHIRE.
  26. ↑ Markus Stabrin, Fabian Schoenfeld, Thorsten Wagner, Sabrina Pospich, Christos Gatsogiannis, Stefan Raunser: TranSPHIRE: automated and feedback-optimized on-the-fly processing for cryo-EM. In: Nature Communications. 11. Jahrgang, Nr. 1. Springer Science and Business Media LLC, 11. November 2020, ISSN 2041-1723, S. 5716, doi:10.1038/s41467-020-19513-2, PMID 33177513, PMC 7658977 (freier Volltext), bibcode:2020NatCo..11.5716S.
  27. ↑ crYOLO.
  28. ↑ Phys.org 
  29. ↑ TomoTwin.
  30. ↑ Sebastian Tacke, Philipp Erdmann, Zhexin Wang, Sven Klumpe, Michael Grange, Jürgen Plitzko, Stefan Raunser: A streamlined workflow for automated cryo focused ion beam milling. In: Journal of Structural Biology. 213. Jahrgang, Nr. 3. Elsevier BV, 2021, ISSN 1047-8477, S. 107743, doi:10.1016/j.jsb.2021.107743, PMID 33971286.
  31. ↑ Felipe Merino, Sabrina Pospich, Johanna Funk, Thorsten Wagner, Florian Küllmer, Hans-Dieter Arndt, Peter Bieling, Stefan Raunser: Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM. In: Nature Structural & Molecular Biology. 25. Jahrgang, Nr. 6, Juni 2018, ISSN 1545-9985, S. 528–537, doi:10.1038/s41594-018-0074-0, PMID 29867215 (englisch, nature.com).
  32. ↑ Johanna Funk, Felipe Merino, Matthias Schaks, Klemens Rottner, Stefan Raunser, Peter Bieling: A barbed end interference mechanism reveals how capping protein promotes nucleation in branched actin networks. In: Nature Communications. 12. Jahrgang, Nr. 1, 9. September 2021, ISSN 2041-1723, S. 5329, doi:10.1038/s41467-021-25682-5, PMID 34504078, PMC 8429771 (freier Volltext), bibcode:2021NatCo..12.5329F (englisch).
  33. ↑ Alexander Belyy, Felipe Merino, Undine Mechold, Stefan Raunser: Mechanism of actin-dependent activation of nucleotidyl cyclase toxins from bacterial human pathogens. In: Nature Communications. 12. Jahrgang, Nr. 1, 16. November 2021, ISSN 2041-1723, S. 6628, doi:10.1038/s41467-021-26889-2, PMID 34785651, PMC 8595890 (freier Volltext), bibcode:2021NatCo..12.6628B (englisch).
  34. ↑ Alexander Belyy, Florian Lindemann, Daniel Roderer, Johanna Funk, Benjamin Bardiaux, Jonas Protze, Peter Bieling, Hartmut Oschkinat, Stefan Raunser: Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin. In: Nature Communications. 13. Jahrgang, Nr. 1, 20. Juli 2022, ISSN 2041-1723, S. 4202, doi:10.1038/s41467-022-31836-w, PMID 35858890, PMC 9300711 (freier Volltext), bibcode:2022NatCo..13.4202B (englisch).
  35. ↑ Sabrina Pospich, Florian Küllmer, Veselin Nasufović, Johanna Funk, Alexander Belyy, Peter Bieling, Hans‐Dieter Arndt, Stefan Raunser: Cryo‐EM Resolves Molecular Recognition Of An Optojasp Photoswitch Bound To Actin Filaments In Both Switch States. In: Angewandte Chemie International Edition. 60. Jahrgang, Nr. 16. Wiley, 4. März 2021, ISSN 1433-7851, S. 8678–8682, doi:10.1002/anie.202013193, PMID 33449370, PMC 8048601 (freier Volltext).
  36. ↑ Alexander Belyy, Felipe Merino, Oleg Sitsel, Stefan Raunser: Structure of the Lifeact–F-actin complex. In: PLOS Biology. 18. Jahrgang, Nr. 11, 20. November 2020, ISSN 1545-7885, S. e3000925, doi:10.1371/journal.pbio.3000925, PMID 33216759, PMC 7717565 (freier Volltext) – (englisch).
  37. ↑ Julian von der Ecken, Mirco Müller, William Lehman, Dietmar J. Manstein, Pawel A. Penczek, Stefan Raunser: Structure of the F-actin–tropomyosin complex. In: Nature. 519. Jahrgang, Nr. 7541. Springer Science and Business Media LLC, 1. Dezember 2014, ISSN 0028-0836, S. 114–117, doi:10.1038/nature14033, PMID 25470062, PMC 4477711 (freier Volltext).
  38. ↑ Max Planck Society: Locating muscle proteins: Scientists bring the basis of muscle movement into sharper focus. In: phys.org. Abgerufen am 14. Oktober 2023 (englisch).
  39. ↑ M. V. S. Import: Was macht Spitzensportler schneller als andere? In: scinexx | Das Wissensmagazin. 24. Juli 2016, abgerufen am 11. August 2023 (deutsch).
  40. ↑ Why is Usain Bolt the fastest person on Earth? In: www.bionity.com. Abgerufen am 14. Oktober 2023 (englisch).
  41. ↑ A pocket full of water molecules. In: www.mpg.de. Abgerufen am 11. August 2023 (englisch).
  42. ↑ Tiniest Details of Actin Filaments Revealed. In: Cell Science from Technology Networks. Abgerufen am 14. Oktober 2023 (englisch).
  43. ↑ Through the backdoor: How phosphate escapes from actin. In: EurekAlert! Abgerufen am 14. Oktober 2023 (englisch).
  44. ↑ Pilar Cossio, Glen M. Hocky: Catching actin proteins in action. In: Nature. 611. Jahrgang, Nr. 7935, November 2022, S. 241–243, doi:10.1038/d41586-022-03343-x (englisch, nature.com).
  45. ↑ Through the backdoor: How phosphate escapes from actin. In: EurekAlert! Abgerufen am 11. November 2023 (englisch).
  46. ↑ Scientists produce high-resolution 3D image of sarcomere using electron cryo-tomography. In: News-Medical.net. 25. März 2021, abgerufen am 11. November 2023 (englisch).
  47. ↑ Electron cryo-tomography reveals 3D images of sarcomeres at high resolution. In: AZoLifeSciences.com. 25. März 2021, abgerufen am 11. November 2023 (englisch).
  48. ↑ Wiley Analytical Science Magazine.
  49. ↑ Peter J. Knight: Getting to the heart of thick-filament structure. In: Nature. 1. November 2023, ISSN 0028-0836, doi:10.1038/d41586-023-03307-9 (englisch, nature.com).
  50. ↑ Mirage News: First High-Resolution Image of Muscle Cell Filaments Captured. In: Mirage News. Abgerufen am 11. November 2023 (australisches Englisch).
  51. ↑ Rouslan G. Efremov, Alexander Leitner, Ruedi Aebersold, Stefan Raunser: Architecture and conformational switch mechanism of the ryanodine receptor. In: Nature. 517. Jahrgang, Nr. 7532. Springer Science and Business Media LLC, 1. Dezember 2014, ISSN 0028-0836, S. 39–43, doi:10.1038/nature13916, PMID 25470059.
  52. ↑ Deivanayagabarathy Vinayagam, Dennis Quentin, Jing Yu-Strzelczyk, Oleg Sitsel, Felipe Merino, Markus Stabrin, Oliver Hofnagel, Maolin Yu, Mark W Ledeboer, Georg Nagel, Goran Malojcic, Stefan Raunser: Structural basis of TRPC4 regulation by calmodulin and pharmacological agents. In: eLife. 9. Jahrgang. eLife Sciences Publications, Ltd, 25. November 2020, ISSN 2050-084X, doi:10.7554/elife.60603, PMID 33236980, PMC 7735759 (freier Volltext).
  53. ↑ Tobias Raisch, Andreas Brockmann, Ulrich Ebbinghaus-Kintscher, Jörg Freigang, Oliver Gutbrod, Jan Kubicek, Barbara Maertens, Oliver Hofnagel, Stefan Raunser: Small molecule modulation of the Drosophila Slo channel elucidated by cryo-EM. In: Nature Communications. 12. Jahrgang, Nr. 1. Springer Science and Business Media LLC, 9. Dezember 2021, ISSN 2041-1723, S. 7164, doi:10.1038/s41467-021-27435-w, PMID 34887422, PMC 8660915 (freier Volltext), bibcode:2021NatCo..12.7164R.
  54. ↑ Marc Jansen: Neue Mitglieder 2022: Stefan Raunser (Klasse für Naturwissenschaften und Medizin). In: Nordrhein-Westfälische Akademie der Wissenschaften und der Künste. 15. Dezember 2022, abgerufen am 11. August 2023.
  55. ↑ German National Academy of Sciences Leopoldina Member Stefan Raunser.
  56. ↑ EMBO_facts_figures_2018.
  57. ↑ Neue Mitglieder für das Junge Kolleg. In: Stiftung Mercator. Abgerufen am 11. August 2023 (deutsch).
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