Mutation screen reveals novel variants and expands the phenotypes associated with DYNC1H1

J Neurol. 2015 Sep;262(9):2124-34. doi: 10.1007/s00415-015-7727-2. Epub 2015 Jun 24.

Abstract

Dynein, cytoplasmic 1, heavy chain 1 (DYNC1H1) encodes a necessary subunit of the cytoplasmic dynein complex, which traffics cargo along microtubules. Dominant DYNC1H1 mutations are implicated in neural diseases, including spinal muscular atrophy with lower extremity dominance (SMA-LED), intellectual disability with neuronal migration defects, malformations of cortical development, and Charcot-Marie-Tooth disease, type 2O. We hypothesized that additional variants could be found in these and novel motoneuron and related diseases. Therefore, we analyzed our database of 1024 whole exome sequencing samples of motoneuron and related diseases for novel single nucleotide variations. We filtered these results for significant variants, which were further screened using segregation analysis in available family members. Analysis revealed six novel, rare, and highly conserved variants. Three of these are likely pathogenic and encompass a broad phenotypic spectrum with distinct disease clusters. Our findings suggest that DYNC1H1 variants can cause not only lower, but also upper motor neuron disease. It thus adds DYNC1H1 to the growing list of spastic paraplegia related genes in microtubule-dependent motor protein pathways.

Keywords: DYNC1H1; Epilepsy; Gastric volvulus; Peripheral neuropathy; Spastic paraplegia; Spinal muscular atrophy.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Charcot-Marie-Tooth Disease / genetics*
  • Charcot-Marie-Tooth Disease / pathology
  • Cytoplasmic Dyneins / genetics*
  • DNA Mutational Analysis
  • Humans
  • Motor Neuron Disease / genetics*
  • Motor Neuron Disease / pathology
  • Motor Neurons / pathology
  • Muscle, Skeletal / pathology
  • Mutation*
  • Phenotype*

Substances

  • DYNC1H1 protein, human
  • Cytoplasmic Dyneins