Microtubule Dynamics may Embody a Stationary Bipolarity Forming Mechanism Related to the Prokaryotic Division Site Mechanism (Pole-to-Pole Oscillations).

Cell division mechanisms in eukaryotes and prokaryotes have until recently been seen as being widely different. However, pole-to-pole oscillations of proteins like MinE in prokaryotes are now known to determine the division plane. These protein waves arise through spontaneous pattern forming reaction-diffusion mechanisms, based on cooperative binding of the proteins to a quasistationary matrix (like the cell membrane or DNA). Rather than waves, stationary bipolar pattern formation may arise as well. Some of the involved proteins have eukaryotic homologs (e.g. FtsZ and tubulin), pointing to a possible ancient shared mechanism. Tubulin polymerizes to microtubules in the spindle. Mitotic microtubules are in a highly dynamical state, frequently undergoing rapid shortening (catastrophe), and fragments formed from the microtubule ends are inferred to enhance the destabilization. Here, we show that cooperative binding of such fragments to microtubules may set up a similar pattern forming mechanism as seen in prokaryotes. The result is a spontaneously formed, well controllable, bipolar state of microtubule dynamics in the cell, which may contribute to defining the bipolar spindle.