Prof. Dr. Jörg Tatzelt

Institut für Biochemie und Pathobiochemie
Biochemie Neurodegenerativer Erkrankungen
Tel.: +49-(0)234-32-22429


Various approaches coming from neuropathology, genetics, animal modeling and biophysics have established a crucial role of protein misfolding in the pathogenic process of different neurodegenerative diseases, such as Alzheimer's disease, Parkinson’s disease, polyglutamine expansion diseases and prion diseases. However, there is an ongoing debate about the nature of the harmful proteinaceous species and how toxic conformers selectively damage neuronal populations.

The main aim of our biochemical research is to identify cellular factors and signaling cascades implicated in neuronal integrity and in the pathophysiological alterations leading to neurodegeneration. Our integrative research has a strong focus on the biochemical and cell biological analysis of cellular pathways, which are also of broad neurobiological interest. Specifically, we are employing in vitro, neuronal cell culture, and animal models to focus on four major topics:

  • Cellular mechanisms underlying the formation and toxic activity of aberrant protein conformers
  • Liquid-liquid phase separation and neurodegeneration
  • Signaling pathways induced by neurotoxic conformers
  • Therapeutic strategies for neurodegenerative diseases



  • New insights into the evolution of the prion protein - Read more
  • A role of NEMO in the clearance of protein aggregates by autophagy - Read more
  • This is how protein aggregates can trigger neurogenerative dieseases - Read more
  • Interview with Dr. Fatemeh Mamashli, our new lab member and Georg Forster Research Fellow - Read more

Selected Publications

  • Banik P, Ray K, Kamps J, Chen QY, Luesch H, Winklhofer KF, Tatzelt J. (2024) VCP/p97 mediates nuclear targeting of non-ER-imported prion protein to maintain proteostasis. Life Sci Alliance Apr 3, 2024. doi: 10.26508/lsa.202302456
  • Kamps J, Bader V, Winklhofer KF, Tatzelt J. (2024) Liquid-liquid phase separation of the prion protein is regulated by the octarepeat domain independently of histidines and copper. J Biol Chem Apr 22, 2024. doi: 10.1016/j.jbc.2024.107310
  • Furthmann N, Bader V, Angersbach L, Blusch A, Goel S, Sanchez-Vicente A, Krause LJ, Chaban SA, Grover P, Trinkaus VA, van Well EM, Jaugstetter M, Tschulik K, Damgaard RB, Saft C, Ellrichmann G, Gold R, Koch A, Englert B, Westenberger A, Klein C, Jungbluth L, Sachse C, Behrends C, Glatzel M, Hartl FU, Nakumara K, Christine CW, Huang EJ, Tatzelt J, Winklhofer KF. (2023) NEMO α -Synuclein aggregate interface and acts as an autophagy adapter by co-condensation with p62. Nat. Commun. Dez 19, 2023. doi: 10.1038/s41467-023-44033-0 
  • Polido SA, Stuani C, Voigt A, Banik P, Kamps J, Bader V, Grover P, Krause LJ, Zerr I, Matschke J, Glatzel M, Winklhofer KF, Buratti E, Tatzelt J. (2024) Cross-seeding by prion protein inactivates TDP-43. Brain 2024 Jan 4; 147(1):240-254. doi: 10.1093/brain/awad289
  • Ramos S, Kamps J, Pezzotti S, Winklhofer KF, Tatzelt J, Havenith M. (2023) Hydration make a difference! How to tune protein complexes between liquid-liquid an liquid-solid phase separation. Phys Chem Chem Phys 2023 Oct. 16. doi: 10.1039/d3cp03299j
  • Goel S, Oliva R, Jeganathan S, Bader V, Krause LJ, Kriegler S, Stender ID, Christine CW, Nakamura K, Hoffmann JE, Winter R, Tatzelt J*, Winklhofer KF* (2023) Linear ubiquitination induces NEMO phase separation to activate NF-κB signaling. Life Sci Alliance Jan 31, 2023. doi: 10.26508/lsa.202201607
    * - corresponding author
  • Wu Z, Berlemann LA, Bader V, Sehr DA, Dawin E, Covallero A, Meschede J, Angersbach L, Showkat C, Michaelis JB, Münch C, Rieger B, Namgaladze D, Herrera MG, Fiesel FC, Springer W, Mendes M, Stepien J, Barkovits K, Marcus K, Sickmann A, Dittmar G, Busch KB, Riedel D, Brini M, Tatzelt J, Cali T, Winklhofer KF. (2022) LUBAC assembles a ubiquitin signaling platform at mitochondria for signal amplification and transport of NF-κB to the nucleus. EMBO J. 18: e112006. doi: 10.15252/embj.2022112006.
  • Kamps J, Lin YH, Oliva R, Bader V, Winter R, Winklhofer KF, Tatzelt J. (2021) The N-terminal domain of the prion protein is required and sufficient for liquid-liquid phase separation: A crucial role of the Aβ-binding domain. J Biol Chem 6; 297(1): 100860. doi: 10.1016/j.jbc.2021.10086