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Stefan Raunser
Born1976
Germany, Landau-Palatinate
NationalityGerman
Alma materMax Planck Institute of Biophysics, Goethe University Frankfurt
Known forCryoEM, CryoET, Membrane protein, Toxin, Cytoskeleton, Sarcomere
AwardsGerman Academy of Sciences Leopoldina
EMBO Member
Einstein Foundation Berlin Professorship
Jugend forscht
Scientific career
FieldsBiochemistry
InstitutionsMax Planck Institute of Molecular Physiology, Harvard Medical School, Freie Universität Berlin, TU Dortmund University, University of Duisburg-Essen
Doctoral advisorProf. Dr. Werner Kühlbrandt[1]
Other academic advisorsProf. Dr. Roger S. Goody, Prof. Dr. Thomas Walz[2]
Websitehttps://www.mpi-dortmund.mpg.de/research/departments/structural-biochemistry

Stefan Raunser[3] (born 1976[4] 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[5] in Dortmund, Germany.

Education and career

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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.[6]

He continued his research as a postdoctoral researcher at Harvard Medical School in Boston, USA, working with Thomas Walz[7] from 2005 to 2008. He then became an "Emmy Noether group leader"[8] at the Max Planck Institute of Molecular Physiology in Dortmund, serving in that position from 2008 to 2013.[9] In 2014, Raunser held the Einstein Professorship[10] 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.[11] In 2015, he became an honorary professor at the University of Duisburg-Essen,[12] and later that same year, he became an adjunct professor at Technical University of Dortmund.[13]

Research and selected publications

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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

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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,[14] his research has focused on molecular mechanisms involved in toxin activation,[15] toxin release,[16] receptor binding,[17][18] membrane permeation,[19] protein translocation,[20][21] and intoxication.[22] His group published a movie of the intoxication process.[23] 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.[24][25]

Software and hardware development in cryoEM/cryoET

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The Raunser lab has contributed to developments in cryoEM image processing and cryoET hardware development.[26] They developed SPHIRE[27] (together with Pawel Penczek), which evolved later into TranSPHIRE.[28] 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[29] and TomoTwin,[30][31] 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.[32]

Structural biochemistry of the cytoskeleton and muscle contraction

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Single particle approach

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Raunser's group has increased the resolution limits of single particle cryoEM reconstructions of muscle and cytoskeletal proteins, including actin filaments (F-actin),[33][34] actin filaments in complex with actin-binding proteins,[35] toxins[36][37] and ligands,[38][39] the actin-tropomyosin complex,[40] and the actomyosin complex.[41][42][43] 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[44][45][46][47] and phosphate release from the filament after hydrolysis.[48]

Tomography approach

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Raunser's group has revealed the three-dimensional organization of the sarcomere in situ,[49][50] 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,[51] and has successfully obtained the world's first high-resolution 3D image of the myosin thick filament in its natural cellular environment.[52][53]

Structural biochemistry of membrane proteins

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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[54] and the TRPC4 channel,[55] as well as the Drosophila's Slowpoke (Slo) potassium channel.[56] This research has provided insights into the regulatory mechanisms and revealed potential target sites for drug development.

Fellowships and awards (selection)

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References

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  1. ^ "Mitglieder".
  2. ^ "Thomas Walz".
  3. ^ "Stefan Raunser Orcid".
  4. ^ "Stefan Raunser Max Planck Institute".
  5. ^ "Raunser".
  6. ^ "Website of the Max Planck Institute of Molecular Physiology" (PDF).
  7. ^ "Thomas Walz Lab HHMI page".
  8. ^ "Emmy Noether Programme". www.dfg.de. Retrieved 2023-08-03.
  9. ^ a b "DFG - GEPRIS - Molecular regulation of cholesterol concentration in cell membranes". gepris.dfg.de. Retrieved 2023-08-03.
  10. ^ a b "Einstein Foundation Professorship - Stefan Raunser".
  11. ^ "Max Planck Institute Dortmund - Director Stefan Raunser".
  12. ^ "University of Duisburg-Essen - Honorary Professor Stefan Raunser".
  13. ^ "TU Dortmund - Professor Stefan Raunser".
  14. ^ Roderer, Daniel; Raunser, Stefan (2019-09-08). "Tc Toxin Complexes: Assembly, Membrane Permeation, and Protein Translocation". Annual Review of Microbiology. 73 (1): 247–265. doi:10.1146/annurev-micro-102215-095531. ISSN 0066-4227. PMID 31140906. S2CID 169033606.
  15. ^ Society, Max Planck. "Researchers decode the toxin complex of the plague bacterium and other germs". phys.org. Retrieved 2023-11-11.
  16. ^ Sitsel, Oleg; Wang, Zhexin; Janning, Petra; Kroczek, Lara; Wagner, Thorsten; Raunser, Stefan (2023). "preprint article on bioRxiv". doi:10.1101/2023.02.22.529496. S2CID 257154745. {{cite journal}}: Cite journal requires |journal= (help)
  17. ^ Roderer, Daniel; Bröcker, Felix; Sitsel, Oleg; Kaplonek, Paulina; Leidreiter, Franziska; Seeberger, Peter H.; Raunser, Stefan (2020). "Glycan-dependent cell adhesion mechanism of Tc toxins". Nature Communications. 11 (1). Springer Science and Business Media LLC: 2694. Bibcode:2020NatCo..11.2694R. doi:10.1038/s41467-020-16536-7. ISSN 2041-1723. PMC 7264150. PMID 32483155.
  18. ^ Xu, Ying; Viswanatha, Raghuvir; Sitsel, Oleg; Roderer, Daniel; Zhao, Haifang; Ashwood, Christopher; Voelcker, Cecilia; Tian, Songhai; Raunser, Stefan; Perrimon, Norbert; Dong, Min (October 2022). "CRISPR screens in Drosophila cells identify Vsg as a Tc toxin receptor". Nature. 610 (7931): 349–355. Bibcode:2022Natur.610..349X. doi:10.1038/s41586-022-05250-7. ISSN 1476-4687. PMC 9631961. PMID 36171290.
  19. ^ Gatsogiannis, Christos; Merino, Felipe; Prumbaum, Daniel; Roderer, Daniel; Leidreiter, Franziska; Meusch, Dominic; Raunser, Stefan (October 2016). "Membrane insertion of a Tc toxin in near-atomic detail". Nature Structural & Molecular Biology. 23 (10): 884–890. doi:10.1038/nsmb.3281. ISSN 1545-9985. PMID 27571177. S2CID 42128471.
  20. ^ Meusch, Dominic; Gatsogiannis, Christos; Efremov, Rouslan G.; Lang, Alexander E.; Hofnagel, Oliver; Vetter, Ingrid R.; Aktories, Klaus; Raunser, Stefan (23 Feb 2014). "Mechanism of Tc toxin action revealed in molecular detail". Nature. 508 (7494). Springer Science and Business Media LLC: 61–65. Bibcode:2014Natur.508...61M. doi:10.1038/nature13015. ISSN 0028-0836. PMID 24572368. S2CID 4462402.
  21. ^ Society, Max Planck. "Bacteria with vuvuzelas: Microbes use a channel protein as a syringe for toxins". phys.org. Retrieved 2023-11-11.
  22. ^ "Mechanism of bacterial toxins in deadly attacks". EurekAlert!. Retrieved 2023-10-14.
  23. ^ Tc toxin mechanism of action, retrieved 2023-08-11
  24. ^ Society, Max Planck. "Protein injections in medicine". phys.org. Retrieved 2023-11-11.
  25. ^ "Protein injections in medicine could one day be possible, says new study". Drug Target Review. Retrieved 2023-11-11.
  26. ^ "ThermoFisher - lab portrait".
  27. ^ "SPHIRE".
  28. ^ Stabrin, Markus; Schoenfeld, Fabian; Wagner, Thorsten; Pospich, Sabrina; Gatsogiannis, Christos; Raunser, Stefan (11 Nov 2020). "TranSPHIRE: automated and feedback-optimized on-the-fly processing for cryo-EM". Nature Communications. 11 (1). Springer Science and Business Media LLC: 5716. Bibcode:2020NatCo..11.5716S. doi:10.1038/s41467-020-19513-2. ISSN 2041-1723. PMC 7658977. PMID 33177513. S2CID 219946743.
  29. ^ "crYOLO".
  30. ^ "Phys.org".
  31. ^ "TomoTwin".
  32. ^ Tacke, Sebastian; Erdmann, Philipp; Wang, Zhexin; Klumpe, Sven; Grange, Michael; Plitzko, Jürgen; Raunser, Stefan (2021). "A streamlined workflow for automated cryo focused ion beam milling". Journal of Structural Biology. 213 (3). Elsevier BV: 107743. doi:10.1016/j.jsb.2021.107743. ISSN 1047-8477. PMID 33971286.
  33. ^ Merino, Felipe; Pospich, Sabrina; Funk, Johanna; Wagner, Thorsten; Küllmer, Florian; Arndt, Hans-Dieter; Bieling, Peter; Raunser, Stefan (June 2018). "Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM". Nature Structural & Molecular Biology. 25 (6): 528–537. doi:10.1038/s41594-018-0074-0. ISSN 1545-9985. PMID 29867215. S2CID 256840705.
  34. ^ Funk, Johanna; Merino, Felipe; Schaks, Matthias; Rottner, Klemens; Raunser, Stefan; Bieling, Peter (2021-09-09). "A barbed end interference mechanism reveals how capping protein promotes nucleation in branched actin networks". Nature Communications. 12 (1): 5329. Bibcode:2021NatCo..12.5329F. doi:10.1038/s41467-021-25682-5. ISSN 2041-1723. PMC 8429771. PMID 34504078.
  35. ^ Belyy, Alexander; Merino, Felipe; Mechold, Undine; Raunser, Stefan (2021-11-16). "Mechanism of actin-dependent activation of nucleotidyl cyclase toxins from bacterial human pathogens". Nature Communications. 12 (1): 6628. Bibcode:2021NatCo..12.6628B. doi:10.1038/s41467-021-26889-2. ISSN 2041-1723. PMC 8595890. PMID 34785651.
  36. ^ Belyy, Alexander; Lindemann, Florian; Roderer, Daniel; Funk, Johanna; Bardiaux, Benjamin; Protze, Jonas; Bieling, Peter; Oschkinat, Hartmut; Raunser, Stefan (2022-07-20). "Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin". Nature Communications. 13 (1): 4202. Bibcode:2022NatCo..13.4202B. doi:10.1038/s41467-022-31836-w. ISSN 2041-1723. PMC 9300711. PMID 35858890.
  37. ^ Pospich, Sabrina; Küllmer, Florian; Nasufović, Veselin; Funk, Johanna; Belyy, Alexander; Bieling, Peter; Arndt, Hans‐Dieter; Raunser, Stefan (4 Mar 2021). "Cryo‐EM Resolves Molecular Recognition Of An Optojasp Photoswitch Bound To Actin Filaments In Both Switch States". Angewandte Chemie International Edition. 60 (16). Wiley: 8678–8682. doi:10.1002/anie.202013193. ISSN 1433-7851. PMC 8048601. PMID 33449370.
  38. ^ Belyy, Alexander; Merino, Felipe; Sitsel, Oleg; Raunser, Stefan (2020-11-20). "Structure of the Lifeact–F-actin complex". PLOS Biology. 18 (11): e3000925. doi:10.1371/journal.pbio.3000925. ISSN 1545-7885. PMC 7717565. PMID 33216759.
  39. ^ von der Ecken, Julian; Müller, Mirco; Lehman, William; Manstein, Dietmar J.; Penczek, Pawel A.; Raunser, Stefan (1 Dec 2014). "Structure of the F-actin–tropomyosin complex". Nature. 519 (7541). Springer Science and Business Media LLC: 114–117. doi:10.1038/nature14033. ISSN 0028-0836. PMC 4477711. PMID 25470062.
  40. ^ Society, Max Planck. "Locating muscle proteins: Scientists bring the basis of muscle movement into sharper focus". phys.org. Retrieved 2023-10-14.
  41. ^ Import, M. V. S. (2016-07-24). "Was macht Spitzensportler schneller als andere?". scinexx | Das Wissensmagazin (in German). Retrieved 2023-08-11.
  42. ^ "Why is Usain Bolt the fastest person on Earth?". www.bionity.com. Retrieved 2023-10-14.
  43. ^ "A pocket full of water molecules". www.mpg.de. Retrieved 2023-08-11.
  44. ^ "Tiniest Details of Actin Filaments Revealed". Cell Science from Technology Networks. Retrieved 2023-10-14.
  45. ^ "Through the backdoor: How phosphate escapes from actin". EurekAlert!. Retrieved 2023-10-14.
  46. ^ Cossio, Pilar; Hocky, Glen M. (November 2022). "Catching actin proteins in action". Nature. 611 (7935): 241–243. doi:10.1038/d41586-022-03343-x.
  47. ^ "Through the backdoor: How phosphate escapes from actin". EurekAlert!. Retrieved 2023-11-11.
  48. ^ "Scientists produce high-resolution 3D image of sarcomere using electron cryo-tomography". News-Medical.net. 2021-03-25. Retrieved 2023-11-11.
  49. ^ "Electron cryo-tomography reveals 3D images of sarcomeres at high resolution". AZoLifeSciences.com. 2021-03-25. Retrieved 2023-11-11.
  50. ^ "Wiley Analytical Science Magazine".
  51. ^ Knight, Peter J. (2023-11-01). "Getting to the heart of thick-filament structure". Nature. doi:10.1038/d41586-023-03307-9. ISSN 0028-0836.
  52. ^ "First High-Resolution Image of Muscle Cell Filaments Captured". Mirage News. Retrieved 2023-11-11.
  53. ^ Efremov, Rouslan G.; Leitner, Alexander; Aebersold, Ruedi; Raunser, Stefan (1 Dec 2014). "Architecture and conformational switch mechanism of the ryanodine receptor". Nature. 517 (7532). Springer Science and Business Media LLC: 39–43. doi:10.1038/nature13916. ISSN 0028-0836. PMID 25470059. S2CID 4383707.
  54. ^ Vinayagam, Deivanayagabarathy; Quentin, Dennis; Yu-Strzelczyk, Jing; Sitsel, Oleg; Merino, Felipe; Stabrin, Markus; Hofnagel, Oliver; Yu, Maolin; Ledeboer, Mark W; Nagel, Georg; Malojcic, Goran; Raunser, Stefan (25 Nov 2020). "Structural basis of TRPC4 regulation by calmodulin and pharmacological agents". eLife. 9. eLife Sciences Publications, Ltd. doi:10.7554/elife.60603. ISSN 2050-084X. PMC 7735759. PMID 33236980.
  55. ^ Raisch, Tobias; Brockmann, Andreas; Ebbinghaus-Kintscher, Ulrich; Freigang, Jörg; Gutbrod, Oliver; Kubicek, Jan; Maertens, Barbara; Hofnagel, Oliver; Raunser, Stefan (9 Dec 2021). "Small molecule modulation of the Drosophila Slo channel elucidated by cryo-EM". Nature Communications. 12 (1). Springer Science and Business Media LLC: 7164. Bibcode:2021NatCo..12.7164R. doi:10.1038/s41467-021-27435-w. ISSN 2041-1723. PMC 8660915. PMID 34887422.
  56. ^ Jansen, Marc (2022-12-15). "Neue Mitglieder 2022: Stefan Raunser (Klasse für Naturwissenschaften und Medizin)". Nordrhein-Westfälische Akademie der Wissenschaften und der Künste (in German). Retrieved 2023-08-11.
  57. ^ "German National Academy of Sciences Leopoldina Member Stefan Raunser".
  58. ^ "EMBO_facts_figures_2018" (PDF).
  59. ^ "Neue Mitglieder für das Junge Kolleg". Stiftung Mercator (in German). Retrieved 2023-08-11.
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