Direct interaction with contactin targets voltage-gated sodium channel Na(v)1.9/NaN to the cell membrane.
J Biol Chem
; 276(49): 46553-61, 2001 Dec 07.
Article
in En
| MEDLINE
| ID: mdl-11581273
ABSTRACT
The mechanisms that target various sodium channels within different regions of the neuronal membrane, which they endow with different physiological properties, are not yet understood. To examine this issue we studied the voltage-gated sodium channel Na(v)1.9/NaN, which is preferentially expressed in small sensory neurons of dorsal root ganglia and trigeminal ganglia and the nonmyelinated axons that arise from them. Our results show that the cell adhesion molecule contactin binds directly to Na(v)1.9/NaN and recruits tenascin to the protein complex in vitro. Na(v)1.9/NaN and contactin co-immunoprecipitate from dorsal root ganglia and transfected Chinese hamster ovary cell line, and co-localize in the C-type neuron soma and along nonmyelinated C-fibers and at nerve endings in the skin. Co-transfection of Chinese hamster ovary cells with Na(v)1.9/NaN and contactin enhances the surface expression of the sodium channel over that of Na(v)1.9/NaN alone. Thus contactin binds directly to Na(v)1.9/NaN and participates in the surface localization of this channel along nonmyelinated axons.
Search on Google
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Neuropeptides
/
Sodium Channels
/
Cell Adhesion Molecules, Neuronal
/
Ion Channel Gating
Limits:
Animals
Language:
En
Journal:
J Biol Chem
Year:
2001
Document type:
Article
Affiliation country:
United States