Rice Lab  

Microtubule dynamics: structure, mechanism, regulation   Microtubule dynamics: structure, mechanism, regulation

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Work in the lab is broadly focused on discovering and quantifying the molecular mechanisms that underlie microtubule dynamics and its regulation by accessory proteins. Our goal is to develop a comprehensive understanding of microtubule dynamics, connecting the properties of individual molecules to the complex polymerization dynamics that emerge - at different length and time scales - from collective interactions among these molecules. As a first step toward this goal, we developed a yeast inducible overexpression system allows us to purify milligram quantities of pure wild-type and mutant yeast αβ-tubulin. The ability to work with purified site-directed αβ-tubulin mutants opens new experimental approaches and breathes new life into established ones.

Our studies draw upon a wide range of techniques: X-ray crystallography, time-lapse microscopy, in vitro reconstitution, yeast genetics, biochemisty, computational modeling, and more. Some of the questions we are currently focused on are:
+ how do TOG-domain-containing regulatory proteins like Stu2p promote fast microtubule elongation?
+ what are the biochemical origins of the very different polymerization dynamics of yeast and animal microtubules?
+ what are the molecular events that lead to catastrophe, the abrupt switch from microtubule elongation to microtubule shrinking?
+ what is the ground state conformation of unpolymerized αβ-tubulin? how do the conformational changes that are required for microtubule incorporation affect the biochemistry of tubulin:tubulin interactions and the microtubue dynamics?

There are more questions we would like to be working on. If you might be interested, check out Join for how to get in touch.