Briefings in Functional Genomics and Proteomics Advance Access published online on February 23, 2006
Briefings in Functional Genomics and Proteomics, doi:10.1093/bfgp/ell002
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* To whom correspondence should be addressed. 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. Joseph G. Gindhart is an associate professor in the Biology Department at the University of Richmond. His research interests are identifying the functions of Drosophila kinesin-1 and the mechanisms of kinesin-cargo attachment.
Paper
Towards an understanding of kinesin-1 dependent transport pathways through the study of protein-protein interactions
Joseph G. Gindhart *
Joseph G. Gindhart, E-mail: jgindhar{at}richmond.edu
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