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FEBS Lett. 2011 Aug 4;585(15):2419-23. doi: 10.1016/j.febslet.2011.06.026. Epub 2011 Jun 26.

Recombinant human cytoplasmic dynein heavy chain 1 and 2: observation of dynein-2 motor activity in vitro.

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Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Tokyo, Japan.


Cytoplasmic dynein is a microtubule (MT) motor protein comprising two classes: dynein-1 and dynein-2. We purified recombinant human dynein-1 and dynein-2 from HEK-293 cells by expressing the streptavidin-binding peptide-tagged human cytoplasmic dynein-1 and dynein-2 heavy chains (HCs), respectively. Electron microscopy of the purified molecules revealed a two-headed structure composed of characteristic dynein motor domains. In an in vitro MT gliding assay, both dynein-1 and dynein-2 showed minus-end-directed motor activities. This is the first demonstration of dynein-2 motor activity, which supports the retrograde intraflagellar transport role of dynein-2. Our expression system of dynein HCs provides a useful means to investigate dynein functions.

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