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.

Cryo-electron microscopy reveals how kinesin-binding protein inhibits microtubule attachment in a subset of kinesins.

Structural, functional, and genetic analyses reveal how kinesin-4 motor KLP-12 precisely modulates the curvature of the microtubule plus-end to inhibit the microtubule dynamics for achieving the proper length control of axons.

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.

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 structural and functional analysis demonstrates the mechanism of dual functional, motility and microtubule depolymerization in a unique motor, KIF19A.

Dynein bypasses obstacles on microtubules more efficiently than single kinesin, and kinesins overcome this limitation when transporting intracellular cargos in teams.

T cell progenitor homing into the thymus requires kindlin-3 to stabilize their adhesion to vascular integrin ligands when blood flow velocities and shear rates increase during development.

Biochemical and genetic approaches reveal how the focal adhesion protein kindlin-2 controls the liver development and homeostasis by reducing inflammation.

Model based on Bayesian cue combination shows that procedural motor learning is driven by perceptual error in localizing one's effector.