Towards an understanding of kinesin-1 dependent transport pathways through the study of protein-protein interactions

Abstract

Kinesin-1 is the founding member of a superfamily of motor proteins that transport macromolecules along microtubules in an ATP-dependent manner. Classic studies show that kinesin-1 binds to intracellular cargos through non-covalent interactions with proteins on the cargo surface, that protein - protein interaction domains are present in the cargo-binding tail domain and that phosphorylation-dependent signal transduction pathways regulate kinesin-cargo interactions. A combination of genetics, biochemistry and proteomics has identified processes in which kinesin-1 has an important role, and helped reveal the mechanisms of kinesin-dependent transport events. These approaches have identified more than 35 proteins that bind to kinesin-1; these proteins act as cargos, cargo receptors and regulators of kinesin-1 activity. This review summarizes our current understanding of kinesin-1 associated proteins, and places those protein-protein interactions into the context of kinesin-1 in vivo function. © 2006 Oxford University Press.