Konecna A, Frischknecht R, Kinter J, Ludwig A, Steuble M, Meskenaite V, Indermühle M, Engel M, Cen C, Mateos JM, Streit P, Sonderegger P (2006)
Publication Type: Journal article
Publication year: 2006
Book Volume: 17
Pages Range: 3651-3663
Journal Issue: 8
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 tabulovesicular organelles to the Kinesin-1 motor. © 2006 by The American Society for Cell Biology.
APA:
Konecna, A., Frischknecht, R., Kinter, J., Ludwig, A., Steuble, M., Meskenaite, V.,... Sonderegger, P. (2006). Calsyntenin-1 docks vesicular cargo to Kinesin-1. Molecular Biology of the Cell, 17(8), 3651-3663. https://doi.org/10.1091/mbc.E06-02-0112
MLA:
Konecna, Anetta, et al. "Calsyntenin-1 docks vesicular cargo to Kinesin-1." Molecular Biology of the Cell 17.8 (2006): 3651-3663.
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