English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/146971
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


Identification of an axonal determinant in the C-terminus of the sodium cannel Na(V)1.2.

AuthorsGarrido Jurado, Juan José ; Fernandes, F.; Giraud, P.; Mouret, I.; Pasqualini, E.; Fache, M. P.; Jullien, F.; Dargent, B.
Keywordsaxonal sorting, endocytosis, hippocampal neuron, ssodium channel
Issue Date2001
PublisherNature Publishing Group
CitationEMBO Journal 20: 5950- 5961 (2001)
AbstractTo obtain a better understanding of how hippocampal neurons selectively target proteins to axons, we assessed whether any of the large cytoplasmic regions of neuronal sodium channel Na(v)1.2 contain sufficient information for axonal compartmentalization. We show that addition of the cytoplasmic C-terminal region of Na(v)1.2 restricted the distribution of a dendritic-axonal reporter protein to axons. The analysis of mutants revealed that a critical segment of nine amino acids encompassing a di-leucine-based motif mediates axonal compartmentalization of chimera. In addition, the Na(v)1.2 C-terminus is recognized by the clathrin endocytic pathway both in non-neuronal cells and the somatodendritic domain of hippocampal neurons. The mutation of the di-leucine motif located within the nine amino acid sequence to alanines resulted in the loss of chimera compartmentalization in axons and of internalization. These data suggest that selective elimination by endocytosis in dendrites may account for the compartmentalized distribution of some proteins in axons.
Identifiersdoi: 10.1093/emboj/20.21.5950
issn: 0261-4189
Appears in Collections:(IC) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.