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In order to perform such diverse activities in the cell, dynein makes use of numerous regulatory partners, including dynactin, LIS1, Nud E and Nud EL [].

Patients with lissencephaly exhibit lamination defects of the cerebral cortex, consistent with a defect in neuronal migration.

They also provide the first evidence for a link between dynein processivity and somal movement, which is essential for proper development of the brain.

Cytoplasmic dynein is a minus-end directed microtubule motor protein involved in a wide variety of functions.

Loa homozygotes showed clear defects in neocortical lamination and neuronal migration resulting from a reduction in the rate of radial migration of bipolar neurons.

These results present a new genetic model for understanding the dynein pathway and its functions during neuronal migration.


However, there are no genetic models with which to study the involvement of dynein directly.

Mice homozygous null for the cytoplasmic dynein heavy chain gene exhibit early embryonic lethality, whereas heterozygotes show no obvious abnormalities [].


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