Priv. Doz. Dr. Günther Woehlke

Microtubules build up one of the systems of the cytoskeleton. For many cellular processes, the filaments have to be re-built and restructured. Apart from polymerization and depolymerization from the ends, internal breaking - termed severing - is an important mechanism. Spastin and katanin are two types of mechanochemical enzymes that use ATP to sever microtubules. We are studying the underlying biophysical mechanism, using fluorescence microscopy and kintetic approaches. Moreover, we are setting up assays to follow the changes in the microtubule lattice that lead to severing. 

For a number of years, we have studied the mechanism of kinesins, motor proteins that carry cellular cargo along microtubule filaments to their sites of destiny. As mechanochemical nanomachines, they, too, couple the chemical energy from ATP hydrolysis to mechanical work. We have studied this process extensively using kinetic and microscopic assays, as well as laser traps and single-molecule fluorescence. The current problems understanding kinesins are regulation and properties of heterodimeric mutants involved in pathogenesis of heterozygous patients.  

For details, see a complete list of our publications.

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Latest Publications


Le D. T. V., Eckert T. and Woehlke G. (2013)
Computer Simulation of Assembly and Co-operativity of Hexameric AAA ATPases
PLOS One, Vol. 8, Issue 7, e67815 [Download]


Eckert T., Le D.T.V., Link S., Friedmann L., Woehlke G. (2013)
Spastin's Microtubule-Binding Properties and Comparison to Katanin
PLoS ONE 7(12) Link:  [download]


T. Eckert, S. Link, D. Tuong-Van Le, J.-P. Sobczak, A. Gieseke, K. Richter and G. Woehlke (2012)
Subunit Interactions and Cooperativity in the Microtubule-severing AAA ATPase Spastin
Journal of Biological Chemistry, doi: 10.1074/jbc.M111.291898 Link:  [download]



Research Area

Motor Proteins
Microtubule Dynamics
Enzyme Mechanism

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