Johannes F. Weijman

This study shows that cargo-sensitive TPR switch in kinesin-1 controls its conformational dynamics by dislocating the TPR shoulder, promoting motor domain activation and microtubule binding.

The paper engineers an allosteric switch in kinesin-1 motors using de novo peptides, showing increased transport in cells through conformational changes.

This study identifies CEP170 as a protein interacting with dynein-2, showing its role in dynein-2 assembly and cilia function through effects on intraflagellar transport and Hedgehog signaling.