Abstract
CYTOPLASMIC dynein is a microtubule-activated ATPase which produces force towards the minus ends of microtubules1,2. It is thought to be responsible for retrograde axonal transport and other aspects of organelle motility2–6 and may have a role in the poleward movement of mitotic chromosomes7,8. Cytoplasmic dynein is an oligomeric complex of two catalytic heavy chains and a number of accessory subunits1,9,10. We now report the cloning and sequencing of a complementary DNA for one of these species, a cytoplasmic dynein-associated polypeptide of relative molecular mass 150,000 (Mr 150K). A full-length cDNA was found to contain an open reading frame of 4.0 kilobases, which is predicted to encode a polypeptide of Mr 145K11. It has extensive homology with the product of the Drosophila gene Glued, which encodes a poly-peptide of Mr 148K11. The Glued mutation is dominant, with pleiotropic developmental defects in heterozygotes and an em-bryonic lethal phenotype in homozygotes. As dominant mutations may involve disruption of normal protein–protein interactions, the Glued mutation should provide insight into the mode of action of cytoplasmic dynein in vivo.
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Holzbaur , E., Hammarback, J., Paschal, B. et al. Homology of a 150K cytoplasmic dynein-associated polypeptide with the Drosophila gene Glued. Nature 351, 579–583 (1991). https://doi.org/10.1038/351579a0
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DOI: https://doi.org/10.1038/351579a0
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