Cytoskeletal proteins

Plasmodium kinesin-8B is essential for male gamete formation and its absence blocks parasite transmission. Using cryo-EM and TIRF, the authors report how kinesin-8B motor domains are tuned to support microtubule motility and depolymerase activity.

While the impact of F-actin architecture on stress transmission is well studied, the role of architecture on stress generation remains unclear. Here authors use in vitro model and show that distinct organizations constrain myosin motion.

In this work the authors report the structure of nucleotide-free kinesin-1 motor domain (apo-KIF5B) in complex with paclitaxel-stabilized microtubules using magic-angle-spinning (MAS) NMR spectroscopy. The study provides insights into the dynamic changes under which the neck linker goes upon binding to ADP.

This paper investigates the origin of two distinct instabilities in active gels of biopolymers and molecular motors. Combining experiments and theory, it shows how to rationally design and control active materials with targeted elasticity and activity.

Planelles-Herrero et al. identify a function for the Elongator complex independent of its enzymatic activity in controlling microtubule stability and generating central spindle asymmetry during asymmetric division in Drosophila.

Cryo-electron microscopy structures of skeletal F-actin show solvent-driven rearrangements governing actin filament assembly and aging with potential application in design of drugs and small molecules for imaging and therapy.