Calsyntenin-1 docks vesicular cargo to kinesin-1.

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.
Mesh Terms:
Amino Acid Sequence, Animals, Calcium-Binding Proteins, Conserved Sequence, Cytoplasmic Vesicles, Growth Cones, HeLa Cells, Humans, Mice, Microtubule-Associated Proteins, Molecular Sequence Data, Mutation, Protein Binding, Protein Transport, Rats, Rats, Sprague-Dawley
Mol. Biol. Cell
Date: Aug. 01, 2006
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