Calsyntenin-1 Docks Vesicular Cargo to Kinesin-1
| Autor: | Peter Sonderegger, Renato Frischknecht, Peter Streit, Marianne Engel, Alexander Ludwig, Martin Steuble, Virginia Meskenaite, Jochen Kinter, Chuan Cen, Anetta Konecna, Martin Indermühle, Jose-Maria Mateos |
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| Přispěvatelé: | University of Zurich, Sonderegger, P |
| Jazyk: | angličtina |
| Rok vydání: | 2006 |
| Předmět: |
Immunoelectron microscopy
Growth Cones Molecular Sequence Data Kinesins Biology 1307 Cell Biology Rats Sprague-Dawley Mice Microtubule 10019 Department of Biochemistry 1312 Molecular Biology Calsyntenin Animals Humans Amino Acid Sequence Growth cone Molecular Biology Conserved Sequence Calcium-Binding Proteins Cytoplasmic Vesicles Cell Biology Articles Anterograde axonal transport Transport protein Cell biology Rats Protein Transport Cytoplasm Mutation 570 Life sciences biology Kinesin Microtubule-Associated Proteins HeLa Cells Protein Binding |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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