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.
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 kinesin-14 motor Kar3 moves along microtubules using a previously undescribed mechanism that critically requires the presence of a non-catalytic head.
Live quantitative monitoring of transcriptional bursting reveals that enhancers responding to different regulators use the same kinetic strategy to produce a complex composite pattern of developmental expression.
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.
The somatic Golgi acts as an asymmetric MTOC within Drosophila neurons, and this, together with the action Kinesin-2, helps maintain minus-end-out microtubule polarity with proximal dendrites.
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.
