Calsyntenin-1 docks vesicular cargo to kinesin-1

Mol Biol Cell. 2006 Aug;17(8):3651-63. doi: 10.1091/mbc.e06-02-0112. Epub 2006 Jun 7.


We identified a direct interaction between the neuronal transmembrane protein calsyntenin-1 and the light chain of Kinesin-1 (KLC1). GST pulldowns demonstrated that two highly conserved segments in the cytoplasmic domain of calsyntenin-1 mediate binding to the tetratricopeptide repeats of KLC1. A complex containing calsyntenin-1 and the Kinesin-1 motor was isolated from developing mouse brain and immunoelectron microscopy located calsyntenin-1 in association with tubulovesicular organelles in axonal fiber tracts. In primary neuronal cultures, calsyntenin-1-containing organelles were aligned along microtubules and partially colocalized with Kinesin-1. Using live imaging, we showed that these organelles are transported along axons with a velocity and processivity typical for fast axonal transport. Point mutations in the two kinesin-binding segments of calsyntenin-1 significantly reduced binding to KLC1 in vitro, and vesicles bearing mutated calsyntenin-1 exhibited a markedly altered anterograde axonal transport. In summary, our results indicate that calsyntenin-1 links a certain type of vesicular and tubulovesicular organelles to the Kinesin-1 motor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium-Binding Proteins / chemistry
  • Calcium-Binding Proteins / metabolism*
  • Conserved Sequence
  • Cytoplasmic Vesicles / metabolism*
  • Growth Cones / metabolism
  • HeLa Cells
  • Humans
  • Mice
  • Microtubule-Associated Proteins / metabolism*
  • Molecular Sequence Data
  • Mutation / genetics
  • Protein Binding
  • Protein Transport
  • Rats
  • Rats, Sprague-Dawley


  • Calcium-Binding Proteins
  • Clstn1 protein, mouse
  • Clstn1 protein, rat
  • Microtubule-Associated Proteins
  • kinesin light-chain proteins