Molecular mechanisms of RNA-binding protein dysfunction in neurodegenerative diseases

Neurodegenerative diseases such as frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) are characterised by insoluble protein aggregates in neurons and glia, which are thought to cause neuronal dysfunction and neurodegeneration. My lab works to understand how proteins become mislocalised and aggregated in neurodegenerative disease. We are interested in understanding how nuclear transport and phase separation are dysregulated in ALS and FTD, and whether these changes can be suppressed by modulating posttranslational modifications.

Research website

Positions held

  • Since 2021: Adjunct Director, Institute of Molecular Biology (IMB) and Professor of Molecular Cell Biology, Faculty of Biology, Johannes Gutenberg University (JGU), Mainz
  • 2014 - 2021: Emmy Noether Group Leader at Ludwig Maximilan University Munich, Biomedical Center (BMC), Cell Biology
  • 2007 - 2014: Postdoctoral Fellow at Ludwig Maximilan University Munich, Adolf-Butenandt Institute


  • 2007: PhD, Rockefeller University, New York
  • 2002: Diploma in Biochemistry, Eberhard Karls University of Tübingen

Selected publications by Dorothee Dormann

Gruijs da Silva LA, Simonetti F, Hutten S, Riemenschneider H, Sternburg EL, Pietrek LM, Gebel J, Dötsch V, Edbauer D, Hummer G, Stelzl LS and Dormann D (2022) Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation. EMBO J, 41:e108443 Link

Zambusi A*, Novoselc KT*, Hutten S, Kalpazidou S, Koupourtidou C, Schieweck R, Aschenbroich S, Silva L, Yazgili AS, van Bebber F, Schmid B, Möller G, Tritscher C, Stigloher C, Delbridge C, Sirko S, Günes ZI, Liebscher S, Schlegel J, Aliee H, Theis F, Meiners S, Kiebler M, Dormann D# and Ninkovic J# (2022) TDP-43 condensates and lipid droplets regulate the reactivity of microglia and regeneration after traumatic brain injury. Nat Neurosci, 25:1608–1625 (*indicates joint contribution, #indicates joint correspondence) Link

Hutten S, Usluer S, Bourgeois B, Simonetti F, Odeh HM, Fare CM, Czuppa M, Hruska-Plochan M, Hofweber M, Polymenidou M, Shorter J, Edbauer D, Madl T and Dormann D (2020) Nuclear import receptors directly bind to arginine-rich dipeptide repeat proteins and suppress their pathological interactionsCell Rep, 33:108538 Link

Alberti S and Dormann D (2019) Liquid-liquid phase separation in diseaseAnnu Rev Genet, 53:171–194 Link

Hofweber M, Hutten S, Bourgeois B, Spreitzer E, Niedner-Boblenz A, Schifferer M, Ruepp MD, Simons M, Niessing D, Madl T and Dormann D (2018) Phase separation of FUS is suppressed by its nuclear import receptor and arginine methylationCell, 173:706-719.e13 Link