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Structural Aspects of the Tubulin Code

David Sept, University of Michigan
Tuesday April 14, 12-1pm
Zoom Link:Ìý
In Person: 550 Sherbrooke, Room 189

Abstract:ÌýMicrotubules are key members of the eukaryotic cytoskeleton and they play a role in a wide range of cellular functions, including transport, motility, and mitosis. These filaments are formed by the polymerization of the protein tubulin and their functions are largely mediated by the binding and action of many different microtubule-binding proteins or MAPs. Over the last decade or so, there has been a growing understanding of how the many tubulin isotypes as well as post-translational modifications — what is commonly termed the tubulin code, influence the structure, dynamics and interactions of tubulin and microtubules. Since most of the isotype sequence differences fall in unstructured parts of the protein, this system is ideal for studying using molecular simulations. In this talk I will present some of our recent work in this area and show how these localized isotype differences manifest themselves in both microtubule function and dynamics.