DYNC1H1 and Charcot-Marie-Tooth disease: For example, a missense mutation that changes an amino acid within the homodimerization domain of Dync1h1 has been found in affected members of a family diagnosed with a dominant, axonal form of Charcot-Marie-Tooth (CMT) Disease [2] that is characterized by distal muscle weakness and atrophy, and mutations of the p150Glued subunit of Dynactin, which interacts with Dync1h1, have been identified in families with slowly progressive lower motor neuron disease and amyotrophic lateral sclerosis [3,4].