Towards an understanding of kinesin-1 dependent transport pathways through the study of protein-protein interactions.
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.
Gindhart
Joseph G
JG
Department of Biology, University of Richmond, 28 Westhampton Way, Richmond, VA 23173, USA. jgindhar@richmond.edu
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001692:Biological Transport; D006801:Humans; D016547:Kinesins / Q000235:genetics / Q000378:metabolism*; D013058:Mass Spectrometry; D008870:Microtubules / Q000502:physiology*; D020409:Molecular Motor Proteins / Q000502:physiology*; D011485:Protein Binding; D020798:Two-Hybrid System Techniques
D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D016547:Kinesins