Göttinger Graduiertenzentrum für Neurowissenschaften, Biophysik und Molekulare Biowissenschaften

Jakobs, Stefan, Prof. Dr.

Professor of High Resolution Microscopy of the Cell


  • 1995 - Diploma, University of Kaiserslautern
  • 1995 - 1999 Graduate studies (MPI for Plant Breeding Research, Cologne, Germany and John-Innes-Centre, Norwich, GB)
  • 1999 Dr. rer. nat. University of Cologne
  • 1999 Postdoc (Laboratory of J. Schell/K. Palme, MPI for Plant Breeding Research, Cologne)
  • 1999 - 2005 Postdoc (MPI for Biophysical Chemistry, Laboratory of S.W. Hell)
  • 2005 - Research group leader at the MPI for Biophysical Chemistry
  • 2007 - Habilitation (Botany/Cell Biology) at the Georg-August-University Göttingen
  • since 2010 - Professor for High Resolution Microscopy of the Cell, University of Göttingen Medical School, Dep. of Neurology




Major Research Interests

Our two major research interests are the investigation of the nanoscale architecture and dynamics of mitochondria and the analysis of reversibly switchable fluorescent proteins (RSFPs) as probes for super-resolution microscopy. Mitochondria are essential organelles in all eukaryotic cells and their dysfunction is involved in many devastating (neurodegenerative) diseases. We want to understand the organization of mitochondria on the nanoscale in healthy and challenged cells and investigate the molecular mechanisms that determine their intricate structure. We utilize a wide array of techniques, including molecular biology, biochemical methods as well as electron and super-resolution microscopy.
RSFPs are fluorescent proteins that may be switched by light between a non-fluorescent and a fluorescent state. Their unique properties open up numerous applications in microscopy and cell biology. We investigate the molecular switching mechanisms and aim to improve the properties of these fascinating proteins as probes for live-cell super-resolution microscopy



Homepage Department/Research Group

https://www.mpinat.mpg.de/jakobs



Selected Recent Publications



  • Stephan T, Brüser C, Deckers M, Steyer AM, Balzarotti F, Barbot M, Behr TS, Heim G, Hübner W, Ilgen P, Lange F, Pacheu‐Grau D, Pape JK, Stoldt S, Huser T, Hell SW, Möbius W, Rehling P, Riedel D, Jakobs S (2020) MICOS assembly controls mitochondrial inner membrane remodeling and crista junction redistribution to mediate cristae formation. EMBO J 39: e104105

  • Stoldt S, Stephan T, Jans DC, Brüser C, Lange F, Keller-Findeisen J, Riedel D, Hell SW, Jakobs S (2019) Mic60 exhibits a coordinated clustered distribution along and across yeast and mammalian mitochondria. PNAS 116 (20): 9853-9858

  • Stephan T, Roesch A, Riedel D, Jakobs S (2019) Live-cell STED nanoscopy of mitochondrial cristae, Scientific Reports 9, pp: 12419

  • Kamper M, Ta H, Jensen NA, Hell SW, Jakobs S (2018) Near-infrared STED nanoscopy with an engineered bacterial phytochrome. Nat Commun 9: 4762

  • Stoldt S, Wenzel D, Kehrein K, Riedel D, Ott M, Jakobs S (2018) Spatial orchestration of mitochondrial translation and OXPHOS complex assembly. Nat Cell Biol 20: 528–534

  • Große L, Wurm CA, Brüser C, Neumann D, Jans DC, Jakobs S (2016) Bax assembles into large ring-like structures remodeling the mitochondrial outer membrane in apoptosis, EMBO J 35 (4), 402-413

  • Jans DC,Wurm CA, Riedel D, Wenzel D, Stagge F, Deckers M, Rehling P and Jakobs S (2013) STED super-resolution microscopy reveals an array of MINOS clusters along human mitochondria, PNAS 110 (22), 8936-8941

  • Grotjohann T, Testa I, Reuss M, Brakemann T, Eggeling C, Hell SW, Jakobs S (2012) rsEGFP2 enables fast RESOLFT nanoscopy of living cells. Elife 1: e00248

  • Brakemann T, Stiel AC, Weber G, Andresen M ,Testa I, Grotjohann T, Leutenegger M, Plessmann U, Urlaub H, Eggeling C, Wahl MC, Hell SW and Jakobs S (2011) A reversibly photoswitchable GFP-like protein with fluorescence excitation decoupled from switching, Nature Biotech. 29 (10), 942-947

  • Wurm CA, Neumann D, Lauterbach MA, Harke B, Egner A, Hell SW, Jakobs S (2011) Nanoscale distribution of mitochondrial import receptor Tom20 is adjusted to cellular conditions and exhibits an inner-cellular gradient. Proc Natl Acad Sci USA 108: 13546-13551