title: Ocsyn and mitochondrial-canalicular complexes in vestibular hair cells.
abstract: Ocsyn, a syntaxin-interacting protein characterized by Safieddine et al. [Safieddine, S., Ly, C.D., Wang, Y.-X., Kachar, B., Petralia, R.S., Wenthold, R.J., 2002. Ocsyn, a novel syntaxin-interacting protein enriched in the subapical region of inner hair cells. Mol. Cell. Neurosci., 20, 343-353] in the guinea pig organ of Corti was primarily identified in organelles located at the subapical region of inner hair cells. They proposed that in cochlear inner hair cells, ocsyn was involved in protein trafficking associated to recycling endosomes. Ocsyn happens to be highly homologous to syntabulin with an almost identical syntaxin-binding domain. Syntabulin is believed to attach syntaxin-containing vesicles to kinesin for their axonal transport along microtubules. The present study shows the distribution of ocsyn in guinea pig and rat vestibular hair cells using immunocytochemistry and confocal microscopy. Ocsyn was characterized by intense immunolabeled spots distributed exclusively in type I and II vestibular hair cells. The subcuticular region under the cuticular plate exhibited particularly densely packed spots. In the neck region of the sensory cells, where microtubules are abundant, there was no colocalization of ocsyn and alpha-tubulin. Ocsyn labeled spots were also present in the medial and basal hair cell regions, particularly in the supranuclear and infranuclear regions. Mitochondria are particularly numerous in these three regions (subcuticular, supranuclear and infranuclear). Double labeling of ocsyn and cytochrome c showed that ocsyn was present in the same zones that mitochondria. This, together with the great similarity of ocsyn and syntabulin, suggest that, akin to syntabulin, ocsyn is involved in addressing organelles. We propose that ocsyn is involved in the formation of the canalicular-mitochondrial complexes depicted by Spicer et al. [Spicer, S.S., Thomopoulos, G.N., Schulte, B.A., 1999. Novel membranous structures in apical and basal compartments of inner hear cells. J. Comp. Neurol., 409, 424-437].
authors.affiliation: INSERM U343, Université de Montpellier II, CC 103, Place Bataillon, 34095, Montpellier, cedex 5, France. Jean.Vautrin@univ-montp2.fr
authors.forename: Jean
authors.initials: J
authors.lastname: Vautrin
authors.forename: Cécile
authors.initials: C
authors.lastname: Travo
authors.forename: Catherine
authors.initials: C
authors.lastname: Boyer
authors.forename: Stéphanie
authors.initials: S
authors.lastname: Ventéo
authors.forename: Daniel
authors.initials: D
authors.lastname: Favre
authors.forename: Claude J
authors.initials: CJ
authors.lastname: Dechesne
mesh_terms: D000818:Animals; D015153:Blotting, Western; D002352:Carrier Proteins / Q000378:metabolism*; D045304:Cytochromes c / Q000378:metabolism; D006168:Guinea Pigs; D018069:Hair Cells, Vestibular / Q000378:metabolism* / Q000648:ultrastructure*; D007150:Immunohistochemistry; D018613:Microscopy, Confocal; D008854:Microscopy, Electron; D008870:Microtubules / Q000378:metabolism / Q000648:ultrastructure; D008928:Mitochondria / Q000648:ultrastructure*; D051381:Rats; D014018:Tissue Distribution
chemical_list: D002352:Carrier Proteins; D045304:Cytochromes c