A TOG:αβ-tubulin Complex Structure Reveals Conformation-Based Mechanisms for a Microtubule Polymerase

Abstract

All TOGether Now αβ-Tubulin is the polymerizing subunit of microtubules, which are dynamic polymers that have essential roles in cell division and intracellular organization. TOG domains are αβ-tubulin binding modules that occur in the evolutionarily conserved Stu2p/XMAP215 family of proteins and promote microtubule elongation. Ayaz et al. (p. 857 ) used crystallographic and biochemical experiments to reveal that the TOG1 domain interacts with guanosine triphosphate–bound αβ-tubulin in a conformation-selective manner, binding preferentially to a “curved,” microtubule-incompatible conformation. The binding mode apparently excludes analogous binding of a second TOG domain to the same heterodimer and may help to ensure polarized growth of microtubules.