In cells, molecular motors called kinesins travel along microtubules to transport cargoes and remodel the cytoskeleton. Overexpression and mutations of the kinesin protein KIF14 have been implicated in cancer and other human diseases, but KIF14’s mechanism of action remains unclear.

In a study published online on June 15 in Nature Communications, a team led by Hernando Sosa, Ph.D., used cryogenic electron microscopy to create the first near-atomic-resolution 3D images showing KIF14 in various dynamic states as it interacts with a microtubule. The images reveal that KIF14’s structure changes as the kinesin binds to and travels along microtubules. These results could lead to strategies for preventing or treating cancers by inhibiting KIF14 activity.

Dr. Sosa is a professor of physiology & biophysics at Einstein. The study’s first author is Matthieu Benoit, Ph.D., who is an associate of physiology & biophysics at Einstein.