For almost fifty years, cell biologists have observed sites in cells where actin and microtubule localizations appear to coincide ultimately leading to diverse cellular functions, physiological processes, and cellular morphologies. The coordinated and often reciprocal relationships of these cytoskeletal systems are defined through physical interactions, polymer end-directed mechanisms at the leading edge and focal adhesions, subunit availability, and complex signaling cascades. However, actin filaments and microtubules do not interact on their own, and require additional proteins to execute coordinated behaviors. Many proteins and cellular signals that mediate actin–microtubule interactions are known, yet exciting new modes of behavior are still being discovered!

 

Our research focuses on the mechanisms that coordinate the dynamic rearrangements of the actin and microtubule cytoskeletons by reconsidering the roles of classic cytoskeletal regulators in regulating the "other" polymer system or both simultaneously. We focus on collaborative mechanisms of actin-microtubule crosstalk initiated at actin filament and microtubule plus-end associated proteins and cell- and in vitro biochemistry-based tools to dechiper these mechanisms.