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.

Genetic suppressor screens with C. elegans reveal a novel function for the Death Associated Protein Kinase in regulation of epithelial microtubule dynamics.

Doublecortin-like kinase 1 modulates its own kinase activity to tune its microtubule-binding affinity, providing molecular insights into a unique form of autoregulatory control over microtubule-binding activity.

Severing axons in C. elegans reveals a mechanism by which the axons sense acute damage and respond by sequential remodeling of their microtubule cytoskeleton.

In vitro reconstitution reveals how a system of molecules works together to transport the motor protein dynein to the start of its track.

Centriole integrity is ensured by the connection between the inner scaffold and microtubule triplets through POC16/WDR90 proteins.

The motor domains of dynein are sufficient to crosslink microtubules and slide them antiparallel to each other.

In vitro reconstitution of mRNA motility reveals the basis of directionally biased motion by groups of motors, their response to potential obstacles, and the consequences of reaching microtubule ends.

The presence of cenexin at the old centrosome imposes a functional asymmetry on the mitotic spindle that impacts chromosome alignment and segregation.

Kinesin Kif2C is recruited to DNA damage sites, modulates the mobility and dynamics of DNA damage foci, and promotes DNA double strand break repair.