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Publication : Calsyntenin-1 docks vesicular cargo to kinesin-1.

First Author  Konecna A Year  2006
Journal  Mol Biol Cell Volume  17
Issue  8 Pages  3651-63
PubMed ID  16760430 Mgi Jnum  J:113428
Mgi Id  MGI:3686572 Doi  10.1091/mbc.E06-02-0112
Citation  Konecna A, et al. (2006) Calsyntenin-1 docks vesicular cargo to kinesin-1. Mol Biol Cell 17(8):3651-63
abstractText  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.
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