FXYD3 (Mat-8), a new regulator of Na,K-ATPase
Détails
ID Serval
serval:BIB_4CFE8BE7A7E9
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
FXYD3 (Mat-8), a new regulator of Na,K-ATPase
Périodique
Molecular Biology of the Cell
ISSN
1059-1524 (Print)
Statut éditorial
Publié
Date de publication
05/2005
Volume
16
Numéro
5
Pages
2363-71
Notes
In Vitro
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: May
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: May
Résumé
Four of the seven members of the FXYD protein family have been identified as specific regulators of Na,K-ATPase. In this study, we show that FXYD3, also known as Mat-8, is able to associate with and to modify the transport properties of Na,K-ATPase. In addition to this shared function, FXYD3 displays some uncommon characteristics. First, in contrast to other FXYD proteins, which were shown to be type I membrane proteins, FXYD3 may have a second transmembrane-like domain because of the presence of a noncleavable signal peptide. Second, FXYD3 can associate with Na,K- as well as H,K-ATPases when expressed in Xenopus oocytes. However, in situ (stomach), FXYD3 is associated only with Na,K-ATPase because its expression is restricted to mucous cells in which H,K-ATPase is absent. Coexpressed in Xenopus oocytes, FXYD3 modulates the glycosylation processing of the beta subunit of X,K-ATPase dependent on the presence of the signal peptide. Finally, FXYD3 decreases both the apparent affinity for Na+ and K+ of Na,K-ATPase.
Mots-clé
Amino Acid Sequence
Animals
Cloning, Molecular
Female
Gastric Mucosa/metabolism
Glycosylation
H(+)-K(+)-Exchanging ATPase/chemistry/metabolism
Membrane Proteins/chemistry/genetics/*metabolism
Mice
Molecular Sequence Data
Mutagenesis, Site-Directed
Na(+)-K(+)-Exchanging ATPase/chemistry/*metabolism
Neoplasm Proteins/chemistry/genetics/*metabolism
Oocytes/metabolism
Protein Processing, Post-Translational
Protein Sorting Signals/genetics
Recombinant Proteins/chemistry/genetics/metabolism
Sequence Homology, Amino Acid
Xenopus laevis
Pubmed
Web of science
Création de la notice
24/01/2008 13:28
Dernière modification de la notice
20/08/2019 15:01