CHE-3, a cytosolic dynein heavy chain, is required for sensory cilia structure and function in Caenorhabditis elegans

Dev Biol. 2000 May 15;221(2):295-307. doi: 10.1006/dbio.2000.9686.


Forward genetic screens using novel assays of nematode chemotaxis to soluble compounds identified three independent transposon-insertion mutations in the gene encoding the Caenorhabditis elegans dynein heavy chain (DHC) 1b isoform. These disruptions were mapped and cloned using a newly developed PCR-based transposon display. The mutations were demonstrated to be allelic to the che-3 genetic locus. This isoform of dynein shows temporally and spatially restricted expression in ciliated sensory neurons, and mutants show progressive developmental defects of the chemosensory cilia. These results are consistent with a role for this motor protein in the process of intraflagellar transport; DHC 1b acts in concert with a number of other proteins to establish and maintain the structural integrity of the ciliated sensory endings in C. elegans.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Caenorhabditis elegans / genetics
  • Caenorhabditis elegans / physiology*
  • Chemotaxis / genetics*
  • Cilia / physiology*
  • Cloning, Molecular
  • Crosses, Genetic
  • Disorders of Sex Development
  • Dyneins / genetics
  • Dyneins / physiology*
  • Female
  • Flagella / physiology
  • Green Fluorescent Proteins
  • Humans
  • Luminescent Proteins / genetics
  • Male
  • Molecular Sequence Data
  • Mutagenesis, Insertional
  • Neurons / physiology*
  • Phylogeny
  • Polymerase Chain Reaction
  • Protein Isoforms / genetics
  • Protein Isoforms / physiology
  • Recombinant Fusion Proteins / biosynthesis
  • Sequence Alignment
  • Sequence Homology, Amino Acid


  • DNAH12 protein, human
  • Luminescent Proteins
  • Protein Isoforms
  • Recombinant Fusion Proteins
  • Green Fluorescent Proteins
  • Dyneins