Taisei Watanabe

Abstract Product inhibition is a common regulatory feature of ATPases, in which the hydrolysis product suppresses further enzymatic activity. Kinesins are microtubule-dependent ATPases that typically undergo inhibition by ADP, the product of ATP hydrolysis. Here, we show that the Caenorhabditis elegans kinesin-3 KLP-6 is unusually resistant to product inhibition by ADP and continues to move along microtubules at an unreduced speed even in the presence of high ADP concentrations.

Abstract KIF1A/UNC-104, a member of the kinesin super family motor proteins, plays a pivotal role in the axonal transport of synaptic vesicles and their precursors. Drosophila melanogaster UNC-104 (DmUNC-104) is a relatively recently discovered Drosophila kinesin. Although some point mutations that disrupt synapse formation have been identified, the biochemical properties of DmUNC-104 protein have not been investigated.

Abstract The axonal transport of synaptic vesicle precursors relies on KIF1A and UNC-104 ortholog motors. In mammals, KIF1Bβ is also responsible for the axonal transport of synaptic vesicle precursors. Mutations in KIF1A and KIF1Bβ lead to a wide range of neuropathies. While previous studies have revealed the biochemical, biophysical and cell biological properties of KIF1A, and its defects in neurological disorders, the fundamental properties of KIF1Bβ remain elusive.