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Briefings in Functional Genomics and Proteomics Advance Access originally published online on February 23, 2006
Briefings in Functional Genomics and Proteomics 2006 5(1):74-86; doi:10.1093/bfgp/ell002
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© Oxford University Press, 2006, All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

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

Joseph G. Gindhart

Joseph G. Gindhart, Department of Biology, University of Richmond, 28 Westhampton Way, Richmond, VA 23173, USA. Tel: (804) 287 6892; Fax: (804) 289 8233; E-mail: jgindhar{at}richmond.edu

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.

Keywords: kinesin, microtubule motors, intracellular transport, yeast two-hybrid system, mass spectrometry, genetic interaction screens


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