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A more recent version of this article appeared on May 1, 2005
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Submitted on October 7, 2004
Revised on February 8, 2005
Accepted on February 19, 2005
Department of Pharmacology and Toxicology, University of Lausanne, CH-1005 Lausanne, Switzerland
Monitoring Editor: Guido Guidotti
Four out of the 7 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 since 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 
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.
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