ABSTRACT
The Kinesin-3 motor domain contains a characteristic stretch of lysine residues in Loop 12, known as the K-loop. Kinesin-3s are a family of transporters and most of their members are implicated in long-distance cargo transport. Regulation by monomer-to-dimer switch is mediated by intramolecular interactions between the neck and tail regions, that hold the kinesin in a monomeric, inactive state. Upon cargo binding, the intramolecular interaction between the neck and tail regions is disrupted and these motors dimerise. Tubulin undergoes a diverse range of post-translational modifications, usually after it polymerises into microtubules. Kinesin-3 interaction with microtubules can also be regulated via the presence of other microtubule-associated proteins. Mutations identified in Kinesin-3 family members cause hereditary spastic paraplegia and related disorders, such as type 2 hereditary sensory and autonomic neuropathy and progressive encephalopathy with oedema, hypsarrhythmia and optic atrophy syndrome.
