An under-studied microtubule-associated protein is found to regulate axon growth and branching by modulating microtubule-based organelle transport through its dual interactions with microtubules and the conventional kinesin motor.
Biochemical and genetic approaches show that the XMAP215 homolog Stu2 directly interacts with the small gamma-tubulin complex and its recruitment factor Spc72 to instigate functions in cytoplasmic microtubule organization.
Microtubules are nucleated by the centrosome of the primary cilium in the apical end-foot of neuroepithelial cells and inter-dependent microtubule and actin dynamics are required here to orchestrate delamination of newborn neurons.
Binding of two macromolecular complexes allows kinetochores to capture force produced by the depolymerising ends of microtubules, allowing chromosomes to be transmitted from a mother cell to its two daughters.
oMAP4 is a microtubule crosslinker that restricts motor driven microtubule motility and cooperates with microtubule motors in the establishment of paraxial microtubule arrangements in differentiating muscle cells.