Göttinger Graduiertenschule für Neurowissenschaften, Biophysik und Molekulare Biowissenschaften

Eckermann, Katrin, Dr. *


  • since 2007 Postdoctoral research, University Medical Center Goettingen (Germany)
  • 2002-2007 Postdoctoral research, Max-Planck Unit Hamburg (Germany)
  • 2002 PhD, University Medical Center Hannover (Germany)
  • 1999 Diploma in Biochemistry, University of Hannover (Germany)



Major Research Interests

Aggregation and fibril formation of proteins are the neuropathological hallmarks of several neurodegenerative diseases such as Parkinson's disease (PD) and Alzheimer's disease (AD). Despite intensive research, the molecular mechanisms underlying these processes and the biochemical nature of the disease-associated toxic species are largely unknown. Our group focuses on unraveling molecular mechanisms of pathological protein aggregation from a biochemical perspective. We investigate biochemical properties of the disease-associated proteins alpha-synuclein and tau in cell culture and animal models. Posttranslational modifications (PTMs) of proteins impact on protein conformation, function, and protein interactions. PTMs are key regulatory events in living cells, and moreover, are involved in different aspects of neurodegenerative diseases. In this context, the posttranslational conjugation of the small ubiquitin-related modifier (SUMO) to target proteins aroused interest in recent years. Our current research interest is the functional analysis of protein sumoylation. Identification and detailed investigation of modified forms of a protein is a prerequisite for our further understanding of disease mechanisms.


Homepage Department/Research Group

www.baehrlab.med.uni-goettingen.de/staff_eckermann.html



Selected Recent Publications


  • Protein phosphorylation in neurodegeneration: friend or foe? Tenreiro S, Eckermann K, Outeiro TF. Front Mol Neurosci. 2014 May 13;7:42.
  • SUMO and Parkinson's disease. Eckermann K. Neuromolecular Med. 2013 Dec;15(4):737-59.
  • The potential for beta-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy. Mocanu MM, Nissen A, Eckermann K, Khlistunova I, Biernat J, Drexler D, Petrova O, Schönig K, Bujard H, Mandelkow E, Zhou L, Rune G, Mandelkow EM. J Neurosci. 2008;28(3):737-48.
  • Mutant SOD1 detoxification mechanisms in intact single cells. Ganesan S, Rohde G, Eckermann K, Sroka K, Schaefer MK, Dohm CP, Kermer P, Haase G, Wouters F, Bähr M, Weishaupt JH. Cell Death Differ. 2008;15(2):312-21.
  • The beta-propensity of Tau determines aggregation and synaptic loss in inducible mouse models of tauopathy. Eckermann K, Mocanu MM, Khlistunova I, Biernat J, Nissen A, Hofmann A, Schönig K, Bujard H, Haemisch A, Mandelkow E, Zhou L, Rune G, Mandelkow EM. J Biol Chem. 2007 Oct 26;282(43):31755-65.