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FEBS Lett. 2013 Nov 29;587(23):3763-9. doi: 10.1016/j.febslet.2013.09.049. Epub 2013 Oct 22.

Delineation of the TRAK binding regions of the kinesin-1 motor proteins.

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University College London School of Pharmacy, 29/39 Brunswick Square, London WC1N 1AX, United Kingdom.


Understanding specific cargo distribution in differentiated cells is a major challenge. Trafficking kinesin proteins (TRAKs) are kinesin adaptors. They bind the cargo binding domain of kinesin-1 motor proteins forming a link between the motor and their cargoes. To refine the TRAK1/2 binding sites within the kinesin-1 cargo domain, rationally designed C-terminal truncations of KIF5A and KIF5C were generated and their co-association with TRAK1/2 determined by quantitative co-immunoprecipitations following co-expression in mammalian cells. Three contributory regions forming the TRAK2 binding site within KIF5A and KIF5C cargo binding domains were delineated. Differences were found between TRAK1/2 with respect to association with KIF5A.


FEZ1; FRET; Forster resonance energy transfer; GRIP; HAP1; HEK; Huntingtin-associated protein; Intracellular transport; Kinesin; Kinesin adaptor protein; MADD; Mitochondrial trafficking; Motor protein; TRAK; adaptor protein mitogen-activated protein kinase-activating death domain; fasciculation and elongation protein-ζ; glutamate receptor-interacting protein 1; human embryonic kidney; trafficking kinesin protein

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