ABSTRACT
The Kinesin-1 family contains the founding members of the kinesin superfamily. Members of this family are general purpose motor proteins for movement towards the plus end of microtubules. The motor domains consist of a core domain of approximately 340 amino acids, with sites for binding adenosine triphosphate (ATP) and microtubules. The principal function of Kinesin-1 is to move cargo towards the plus end of microtubules. It is exquisitely adapted to accomplish this task as demonstrated by many studies on the motile properties of the isolated protein. A key feature of kinesins in general is that both the ATP-bound state and the no-nucleotide rigour state, but not the ADP state, are tightly bound to microtubules. Members of the Kinesin-1 family play critical roles in diverse processes, from fast axonal transport of membrane-bound organelles down axons and positioning of mitochondria and nuclei to movement of RNA granules, intermediate filaments and even dynein and microtubules.
