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.

Kinesin-like calmodulin-binding protein integrates microtubules and F-actin to assemble the cytoskeletal configuration needed for trichome formation.

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.

Rab6A binds directly to both the C-terminus and the N-terminal motor domain of the kinesin KIF1C to regulate vesicle motility and Golgi organization.

Microtubule attachment fundamentally modifies kinesin's behavior by triggering a ‘clamshell’ opening of the nucleotide cleft, subsequently reversed by ATP binding, that couples to cargo translocation.

The motor protein kinesin utilizes its fuel molecule by active and concerted motions of its subdomains, while it rapidly interacts with the microtubule track by forming a wet and dynamic interface.

Kinesin-4 KIF21B combines a processive motor activity with two non-motor microtubule-binding domains and an autoregulatory region to induce pausing of microtubule plus ends.

A novel algorithm is used to solve the first 3D reconstruction of a stepping kinesin dimer on microtubules, directly visualizing the conformational effects of inter-head strain and giving novel insights into the motility mechanism.

Kindlin-2 co-operates with talin to activate fibronectin-binding integrins on fibroblasts and subsequently induces cell spreading by recruiting paxillin to small, peripheral nascent adhesions.

The Bipolar Assembly domain of kinesin-5 comprises an anti-parallel four-helix bundle, which explains how kinesin-5 subunits assemble into bipolar tetramers with two motile ends that transmit forces while crosslinking and sliding adjacent microtubules during mitosis.