Abstract:
: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.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Konecna A,Frischknecht R,Kinter J,Ludwig A,Steuble M,Meskenaite V,Indermühle M,Engel M,Cen C,Mateos JM,Streit P,Sonderegger Pdoi
10.1091/mbc.e06-02-0112subject
Has Abstractpub_date
2006-08-01 00:00:00pages
3651-63issue
8eissn
1059-1524issn
1939-4586pii
E06-02-0112journal_volume
17pub_type
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