.Proteins and their interaction networks are at the heart of life. Understanding how diverse and complex proteins come together spatially and temporally and how their specific interactions translate into cellular functions represents a major challenge. Our group uses X-ray crystallography in combination with biochemical and biophysical methods to investigate protein interactions implicated in the regulation of the microtubule cytoskeleton. Microtubules are filamentous structures fundamentally involved in many diverse cellular processes ranging from cell division, motility and intracellular transport. Because of its important role for cell viability, malfunction of the microtubule cytoskeleton is associated with many human pathologies including cancer, cardiovascular and neurodegenerative disorders. We are investigating the nature, modes of regulation, and the structural and biophysical properties of protein interaction networks regulating the microtubule cytoskeleton.
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"Molecular mechanism of action of microtubule-stabilizing agents."
Prota, A.E., Bargsten, K., Zurwerra, D., Field, J.J., Díaz, J.F. Altmann, K.-H., Steinmetz, M.O.
Science 339:587-590 (2013)
"Structural basis of the nine-fold symmetry of centrioles."
Kitagawa, D., Vakonakis, I., Olieric, N., Hilbert, M., Keller, D., Olieric, V., Bortfeld, M., Erat, M.C., Flückiger, I., Gönczy, P., Steinmetz, M.O.
Cell 144(3):364-75 (2011)
"An EB1-binding motif acts as a microtubule tip localization signal."
Honnappa S, Montenegro Gouveia S, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJA, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wüthrich K, Akhmanova A and Steinmetz M.O.
Cell 138(2):366-76 (2009)
"Tracking the ends: a dynamic protein network controls the fate of microtubule tips."
Akhmanova A and Steinmetz M.O.
Nature Reviews Molecular Cell Biology 9(4):309-22 (2008)