Les protéines FXYD: nouveaux régulateurs de la Na,K-ATPase [FXYD proteins: novel regulators of Na,K-ATPase]

Détails

ID Serval
serval:BIB_82C4ABC5846D
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
Titre
Les protéines FXYD: nouveaux régulateurs de la Na,K-ATPase [FXYD proteins: novel regulators of Na,K-ATPase]
Périodique
Médecine Sciences
Auteur(s)
Delprat B., Bibert S., Geering K.
ISSN
0767-0974
Statut éditorial
Publié
Date de publication
07/2006
Peer-reviewed
Oui
Volume
22
Numéro
6-7
Pages
633-638
Langue
français
Notes
Publication types: English Abstract ; Journal Article ; Review
Résumé
Members of the FXYD protein family are small membrane proteins which are characterized by an FXYD motif, two conserved glycines and a serine residue. FXYD proteins show a tissue-specific distribution. Recent evidence suggests that 6 out of 7 FXYD proteins, FXYD1 (phospholemman), FXYD2 (gamma subunit of Na,K-ATPase), FXYD3 (Mat-8), FXYD4 (CHIF), FXYD5 (Ric) and FXYD7 associate with Na,K-ATPase and modulate its transport properties e.g. its Na+ and/or its K+ affinity in a distinct way. These results highlight the complex regulation of Na+ and K+ transport which is necessary to ensure proper tissue functions such as renal Na+-reabsorption, muscle contractility and neuronal excitability. Moreover, mutation of a conserved glycine residue into an arginine residue in FXYD2 has been linked to cases of human hypomagnesemia indicating that dysregulation of Na,K-ATPase by FXYD proteins may be implicated in pathophysiological states. A better characterization of this novel regulatory mechanism of Na,K-ATPase may help to better understand its role in physiological and pathophysiological conditions.
Mots-clé
Amino Acid Sequence, Animals, Arginine, Biological Transport, Calcium-Binding Proteins/chemistry, Calcium-Binding Proteins/genetics, Conserved Sequence, Glycine, Homeostasis, Membrane Proteins/chemistry, Membrane Proteins/genetics, Molecular Sequence Data, Potassium/metabolism, Sequence Alignment, Sodium/metabolism, Sodium-Potassium-Exchanging ATPase/chemistry, Sodium-Potassium-Exchanging ATPase/genetics
Pubmed
Web of science
Création de la notice
24/01/2008 13:28
Dernière modification de la notice
20/08/2019 15:42
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