Biochemical, single molecule, cell and structural biology studies reveal an interaction between the kinesin-5 tail and motor domains regulating high-force production, which is critical for microtubule sliding motility.
Synaptic defects previously attributed to loss of kinesin function are found to be mediated by the Wnd/DLK axonal injury signaling pathway, which restrains the total levels of presynaptic proteins in response to their accumulation.
Cryo-electron microscopy reconstructions of two microtubule-bound transport kinesins at 7 Å resolution reveal how microtubule track binding stimulates ADP release, primes the active site for ATP binding and enables force generation.
A theoretical framework for the growth of microtubules quantifies the roles of geometry, mechanics, kinetics and randomness and provides a phase diagram for dynamic instability in these self-assembled polymers.
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.