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Identification of an axonal determinant in the C‐terminus of the sodium channel Na v 1.2
Author(s) -
Garrido Juan José,
Fernandes Fanny,
Giraud Pierre,
Mouret Isabelle,
Pasqualini Eric,
Fache MariePierre,
Jullien Florence,
Dargent Bénédicte
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.21.5950
Subject(s) - biology , microbiology and biotechnology , compartmentalization (fire protection) , endocytic cycle , sodium channel , hippocampal formation , cytoplasm , endocytosis , tyrosine , c terminus , internalization , nav1 , chimera (genetics) , neuron , amino acid , biochemistry , neuroscience , sodium , receptor , chemistry , organic chemistry , gene , enzyme
To 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.