Elongator is a microtubule polymerase selective for polyglutamylated tubulin.

Elongator is a tRNA-modifying complex that regulates protein translation. Recently, a moonlighting function of Elongator has been identified in regulating the polarization of the microtubule cytoskeleton during asymmetric cell division. Elongator induces symmetry breaking of the anaphase midzone by selectively stabilizing microtubules on one side of the spindle, contributing to the downstream polarized segregation of cell-fate determinants, and therefore to cell fate determination. Here, we investigate how Elongator controls microtubule dynamics. Elongator binds both to the tip of microtubules and to free GTP-tubulin heterodimers using two different subcomplexes, Elp123 and Elp456, respectively. We show that these activities must be coupled for Elongator to decrease the tubulin critical concentration for microtubule elongation. As a consequence, Elongator increases the growth speed and decreases the catastrophe rate of microtubules. Surprisingly, the Elp456 subcomplex binds to tubulin tails and has strong selectivity towards polyglutamylated tubulin. Hence, microtubules assembled by Elongator become selectively enriched with polyglutamylated tubulin, as observed in vitro, in mouse and Drosophila cell lines, as well as in vivo in Drosophila Sensory Organ Precursor cells. Therefore, Elongator rewrites the tubulin code of growing microtubules, placing it at the core of cytoskeletal dynamics and polarization during asymmetric cell division.