4 p.m. - 5 p.m. Location: SLC 1.102
Dr. Luke Rice (UT Southwestern)
An important frontier for modern biology is to discover and understand how collective dynamic behaviors are determined by the structural and biochemical properties of the individual components. Work in my lab seeks to solve this problem for one instance of a collective behavior, microtubule polymerization dynamics. Microtubules are hollow, cylindrical polymers built from αβ-tubulin, a complex of two related proteins. Microtubules have essential roles in cells: in non-dividing cells they form ‘rails’ on which cargo can be transported, and in dividing cells they assemble a dynamic structure called the mitotic spindle that ensures faithful segregation of the genetic material into the two daughter cells. Microtubules exhibit a fascinating, non-equilibrium property called ‘dynamic instability’, wherein they switch apparently randomly between sustained phases of elongation or shrinking. Dynamic instability is essential for proper microtubule function, and it is an intrinsic property of the polymerizing αβ-tubulin subunits. Thus, microtubule polymerization dynamics represents a collective behavior that is compositionally simple and that can be studied outside the cell using purified protein. However, and despite over 30 years of study, we still lack a predictive understanding that can connect measureable properties of the polymerizing subunits to the polymerization dynamics they generate. My presentation will provide an introduction to microtubules and their polymerization dynamics, and I will explain how my lab uses computational simulations to translate structural and biochemical properties of individual αβ-tubulins into predictions of microtubule polymerization dynamics. This approach is allowing us to discover and validate meaningful connections between subunit properties and the larger scale kinetic behavior they collectively generate.