FXYD3 (Mat-8), a new regulator of Na,K-ATPase

Details

Serval ID
serval:BIB_4CFE8BE7A7E9
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
FXYD3 (Mat-8), a new regulator of Na,K-ATPase
Journal
Molecular Biology of the Cell
Author(s)
Crambert  G., Li  C., Claeys  D., Geering  K.
ISSN
1059-1524 (Print)
Publication state
Published
Issued date
05/2005
Volume
16
Number
5
Pages
2363-71
Notes
In Vitro
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: May
Abstract
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.
Keywords
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
Create date
24/01/2008 12:28
Last modification date
20/08/2019 14:01
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