The CC1-FHA dimer is essential for KIF1A-mediated axonal transport of synaptic vesicles in C. elegans

Biochem Biophys Res Commun. 2013 Jun 7;435(3):441-6. doi: 10.1016/j.bbrc.2013.05.005. Epub 2013 May 10.


KIF1A, a member of kinesin-3 motors, plays a pivotal role in anterograde axonal transport of synaptic vesicles (SVs). We have shown that the CC1-FHA tandem of KIF1A forms a stable dimer that is crucial for both the dimerization and activation of the motor. However, it remains to be determined whether the CC1-FHA dimer is essential for KIF1A-mediated axonal transport in vivo. Here, we use Caenorhabditis elegans as the model organism to probe the in vivo function of the CC1-FHA dimer. Disruption of the CC1-FHA dimer severely impairs the KIF1A-mediated regulation of the locomotion and pumping behavior of C. elegans and exerts a significant impact on KIF1A-mediated axonal SV transport. Thus, together with previous structural and biochemical studies, the in vivo data presented in this study firmly establish the essential role of the CC1-FHA dimer for KIF1A-mediated neuronal transport.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Animals, Genetically Modified
  • Axonal Transport / genetics*
  • Caenorhabditis elegans / genetics
  • Caenorhabditis elegans / physiology*
  • Caenorhabditis elegans Proteins / chemistry
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / physiology*
  • Movement / physiology
  • Nerve Tissue Proteins / chemistry*
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / physiology*
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Protein Stability
  • Synaptic Vesicles / chemistry*
  • Synaptic Vesicles / genetics


  • Caenorhabditis elegans Proteins
  • Nerve Tissue Proteins
  • UNC-104 protein, C elegans