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First published online 25 August 2009
doi: 10.1242/jcs.050526

Journal of Cell Science 122, 3403-3413 (2009)
Published by The Company of Biologists 2009
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Research Article

Axonal targeting of Caspr2 in hippocampal neurons via selective somatodendritic endocytosis

Christophe Bel1, Ksénia Oguievetskaia2, Christophe Pitaval1, Laurence Goutebroze2 and Catherine Faivre-Sarrailh1,*

1 Centre de Recherche en Neurobiologie et Neurophysiologie de Marseille, UMR 6231 CNRS, Université de la Méditerranée Aix-Marseille II, Marseille 13916, France
2 Unité Mixte de Recherche-S 839, Inserm, Université Pierre et Marie Curie, Institut du Fer à Moulin, Paris 75005, France

* Author for correspondence (catherine.sarrailh{at}univmed.fr)

Accepted 13 July 2009

Contactin-associated protein 2 (Caspr2) is a neuronal membrane protein that is mutated in autism and related disorders. Although it is highly enriched at juxtaparanodes of Ranvier where it is essential for Shaker-type K+ channel clustering, little is known about its function and regulation. In the present study, we examined the polarized expression of Caspr2 in hippocampal neurons using extracellular hemagglutinin (HA)-tagged Caspr2 constructs. We found that Caspr2 was targeted to the axonal surface, but colocalized with early endosomes in the somatodendritic compartment. The inhibition of endocytosis using a Dynamin-1 mutant or treatment with Dynasore prevented Caspr2 internalization from the dendrites and cell body. We identified a short sequence included into the 4.1B-binding domain that is required for the endocytosis of Caspr2. This sequence contains a protein kinase C (PKC) substrate motif on Thr1292, and point mutation of this residue or treatment with a PKC inhibitor prevented the somatodendritic internalization of Caspr2. Thus, the PKC-dependent trafficking of Caspr2 underlies its polarized expression in hippocampal neurons.

Key words: Node of Ranvier, Juxtaparanode, Neuronal polarity, PKC phosphorylation


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