The role of Nedd4/Nedd4-like dependant ubiquitylation in epithelial transport processes

Détails

ID Serval
serval:BIB_A5A57C2EA6A6
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
The role of Nedd4/Nedd4-like dependant ubiquitylation in epithelial transport processes
Périodique
Pflügers Archiv : European Journal of Physiology
Auteur(s)
Flores  S. Y., Debonneville  C., Staub  O.
ISSN
0031-6768 (Print)
Statut éditorial
Publié
Date de publication
06/2003
Volume
446
Numéro
3
Pages
334-338
Résumé
Ubiquitylation has emerged as an important mechanism for controlling surface expression of membrane proteins. This post-translational modification involves the sequential action of several enzymes including a ubiquitin-activating enzyme E1, a ubiquitin-conjugating enzyme E2 and a ubiquitin-protein ligase E3. E3s are responsible for substrate recognition. Here we describe the role of the Nedd4/Nedd4-like family of ubiquitin-protein ligases in the regulation of proteins involved in epithelial transport. The Nedd4/Nedd4-like proteins are composed of a N-terminal C2 domain, several WW domains and a catalytic HECT domain. The epithelial Na(+) channel ENaC is the best studied example of a Nedd4/Nedd4-like substrate. Its cell surface expression is regulated by the ubiquitin-protein ligase Nedd4-2 via direct PY motif/WW domain interaction. This regulatory mechanism is impaired in Liddle's disease, an inherited form of human hypertension, and is controlled by Sgk1, an aldosterone-inducible kinase which phosphorylates Nedd4-2. The regulation of ENaC by Nedd4-2 is a paradigm for the control of epithelial membrane proteins, as evidenced by the regulation of the ClC-5 chloride channel by the ubiquitin-protein ligase WWP2 or the tight junction protein Occludin by Itch.
Mots-clé
Animals Biological Transport/physiology Chloride Channels/metabolism Epithelial Sodium Channel Humans Membrane Proteins/metabolism Sodium Channels/*metabolism Ubiquitin/*metabolism Ubiquitin-Protein Ligases/*physiology
Pubmed
Web of science
Création de la notice
24/01/2008 13:03
Dernière modification de la notice
20/08/2019 15:10
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