The kinesin KIF15 (magenta) bound to the kinesin-binding protein (KIFBP). Design by LSI multimedia designer Rajani Arora; cryo-EM structure provided by Michael Cianfrocco.
Kinesin motor proteins travel along microtubule tracks to deliver their cargo throughout cells. KIFBP, a kinesin-binding protein which is mutated in Goldberg-Shprintzen syndrome, has emerged as an important negative regulator of a subset of kinesin motors. Researchers in the Cianfrocco lab and their collaborators used cryo-electron microscopy and cross-linking mass spectrometry to determine high-resolution structures of KIFBP alone and in complex with two mitotic kinesins. The structures, together with their results from molecular dynamics simulations, biochemical assays, and cell biology, led the team to propose a model in which KIFBP binds to and stabilizes kinesin in a conformation that is incompatible with microtubule binding and sterically inhibits kinesin's microtubule-binding interface.
Research article in Science Advances
News article from the Life Sciences Institute