Epithelial sodium channel/degenerin family of ion channels: a variety of functions for a shared structure.

Détails

ID Serval
serval:BIB_B0EA0AF092AC
Type
Article: article d'un périodique ou d'un magazine.
Sous-type
Synthèse (review): revue aussi complète que possible des connaissances sur un sujet, rédigée à partir de l'analyse exhaustive des travaux publiés.
Collection
Publications
Institution
Titre
Epithelial sodium channel/degenerin family of ion channels: a variety of functions for a shared structure.
Périodique
Physiological Reviews
Auteur⸱e⸱s
Kellenberger S., Schild L.
ISSN
0031-9333[print], 0031-9333[linking]
Statut éditorial
Publié
Date de publication
2002
Volume
82
Numéro
3
Pages
735-767
Langue
anglais
Résumé
The recently discovered epithelial sodium channel (ENaC)/degenerin (DEG) gene family encodes sodium channels involved in various cell functions in metazoans. Subfamilies found in invertebrates or mammals are functionally distinct. The degenerins in Caenorhabditis elegans participate in mechanotransduction in neuronal cells, FaNaC in snails is a ligand-gated channel activated by neuropeptides, and the Drosophila subfamily is expressed in gonads and neurons. In mammals, ENaC mediates Na+ transport in epithelia and is essential for sodium homeostasis. The ASIC genes encode proton-gated cation channels in both the central and peripheral nervous system that could be involved in pain transduction. This review summarizes the physiological roles of the different channels belonging to this family, their biophysical and pharmacological characteristics, and the emerging knowledge of their molecular structure. Although functionally different, the ENaC/DEG family members share functional domains that are involved in the control of channel activity and in the formation of the pore. The functional heterogeneity among the members of the ENaC/DEG channel family provides a unique opportunity to address the molecular basis of basic channel functions such as activation by ligands, mechanotransduction, ionic selectivity, or block by pharmacological ligands.
Mots-clé
Amino Acid Sequence, Animals, Epithelial Sodium Channel, Humans, Ion Channels/chemistry, Ion Channels/genetics, Molecular Sequence Data, Nerve Tissue Proteins/chemistry, Nerve Tissue Proteins/genetics, Sodium Channels/chemistry, Sodium Channels/genetics, Structure-Activity Relationship
Pubmed
Web of science
Création de la notice
24/01/2008 12:45
Dernière modification de la notice
20/08/2019 15:19
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