Abstract
Dynein, an ATPase, is the force-generating protein in cilia and flagella1. It has long been speculated that cytoplasmic microtubules contain a related enzyme involved in cell division2 or in intracellular organelle transport3. A 'cytoplasmic dynein' has been described in sea urchin eggs4,5, but because the egg stockpiles precursors for both cytoplasmic and ciliary microtubules, the role of this enzyme in the cell has remained unresolved. We recently found that the microtubule-associated protein (MAP) 1C (ref. 6) from brain is a microtubule-activated ATPase7 that produces force in the direction corresponding to retrograde organelle transport in the cell8. MAP 1C has several similar properties to ciliary and flagellar dynein7–9. Here we show directly, using scanning transmission electron microscopy, that MAP 1C is structurally equivalent to the ciliary and flagellar enzyme and is the long-sought cytoplasmic analogue of this enzyme.
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Vallee, R., Wall, J., Paschal, B. et al. Microtubule-associated protein 1C from brain is a two-headed cytosolic dynein. Nature 332, 561–563 (1988). https://doi.org/10.1038/332561a0
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DOI: https://doi.org/10.1038/332561a0
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