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MBC in Press, published online ahead of print June 7, 2006
Mol. Biol. Cell 10.1091/mbc.E06-02-0112

A more recent version of this article appeared on August 1, 2006
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Submitted on February 7, 2006
Revised on May 8, 2006
Accepted on May 31, 2006

Calsyntenin-1 Docks Vesicular Cargo to Kinesin-1

Anetta Konecna,*{dagger} Renato Frischknecht,*{dagger}{ddagger} Jochen Kinter,*{dagger} Alexander Ludwig,*{dagger} Martin Steuble,*{dagger} Virginia Meskenaite,* Martin Indermühle,* Marianne Engel,* Chuan Cen,* José-Maria Mateos,{sect} Peter Streit,{sect} and Peter Sonderegger*

*Department of Biochemistry, University of Zurich, CH-8057 Zürich, Switzerland; {sect}Brain Research Institute, University of Zurich, CH-8057 Zürich, Switzerland; {ddagger}Leibniz Institute for Neurobiology, 39 118 Magdeburg, Germany

Monitoring Editor: Randy Schekman

We identified a direct interaction between the neuronal transmembrane protein calsyntenin-1 and the light chain of Kinesin-1 (KLC1). GST pull-downs 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 tubulo-vesicular 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 tubulo-vesicular organelles to the Kinesin-1 motor.

{dagger}These authors contributed equally to this work.

Address correspondence to: Peter Sonderegger (pson{at}bioc.unizh.ch)




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