Phospholemman (FXYD1) associates with Na,K-ATPase and regulates its transport properties

Détails

ID Serval
serval:BIB_0702C08AC4AE
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Phospholemman (FXYD1) associates with Na,K-ATPase and regulates its transport properties
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur(s)
Crambert  G., Fuzesi  M., Garty  H., Karlish  S., Geering  K.
ISSN
0027-8424 (Print)
Statut éditorial
Publié
Date de publication
08/2002
Volume
99
Numéro
17
Pages
11476-81
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Aug 20
Résumé
A family of small, single-span membrane proteins (the FXYD family) has recently been defined based on their sequence and structural homology. Some members of this family have already been identified as tissue-specific regulators of Na,K-ATPase (NKA). In the present study, we demonstrate that phospholemman (PLM) (FXYD1), so far considered to be a heart- and muscle-specific channel or channel-regulating protein, associates specifically and stably with six different alpha-beta isozymes of NKA after coexpression in Xenopus oocytes, and with alpha1-beta, and less efficiently with alpha2-beta isozymes, in native cardiac and skeletal muscles. Stoichiometric association of PLM with NKA occurs posttranslationally either in the Golgi or the plasma membrane. Interaction of PLM with NKA induces a small decrease in the external K+ affinity of alpha1-beta1 and alpha2-beta1 isozymes and a nearly 2-fold decrease in the internal Na+ affinity. In conclusion, this study demonstrates that PLM is a tissue-specific regulator of NKA that may play an essential role in muscle contractility.
Mots-clé
Animals Biological Transport Calcium-Transporting ATPases/metabolism Cattle Cloning, Molecular Dogs Endoplasmic Reticulum/enzymology Female Heart/physiology Humans Kidney/physiology Membrane Potentials Membrane Proteins/genetics/*metabolism Microsomes/metabolism Muscle, Skeletal/physiology Na(+)-K(+)-Exchanging ATPase/*metabolism Oocytes/physiology Phosphoproteins/genetics/*metabolism Protein Subunits Rats Recombinant Proteins/metabolism Sarcoplasmic Reticulum/enzymology Sarcoplasmic Reticulum Calcium-Transporting ATPases Xenopus laevis
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 13:28
Dernière modification de la notice
08/05/2019 14:00
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