RESEARCH: Review of Kinesin dependent axonal transport

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Mark

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Towards an understanding of kinesin-1 dependent

transport pathways through the study of

protein–protein interactions

ph G. Gindhart

ph G. Gindhart, Department of Biology, University

of Richmond, 28 Westhampton Way, Richmond, VA 23173,

USA.

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.

SOURCE: Briefings in Functional Genomics and

Proteomics 2006 5(1):74-86; doi:10.1093/bfgp/ell002

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