FXYD7 is a brain-specific regulator of Na,K-ATPase alpha1-beta isozymes
Open Access
- 1 July 2002
- journal article
- research article
- Published by Springer Nature in The EMBO Journal
- Vol. 21 (13) , 3264-3273
- https://doi.org/10.1093/emboj/cdf330
Abstract
Recently, corticosteroid hormone‐induced factor (CHIF) and the γ‐subunit, two members of the FXYD family of small proteins, have been identified as regulators of renal Na,K‐ATPase. In this study, we have investigated the tissue distribution and the structural and functional properties of FXYD7, another family member which has not yet been characterized. Expressed exclusively in the brain, FXYD7 is a type I membrane protein bearing N‐terminal, post‐translationally added modifications on threonine residues, most probably O ‐glycosylations that are important for protein stabilization. Expressed in Xenopus oocytes, FXYD7 can interact with Na,K‐ATPase α1–β1, α2–β1 and α3–β1 but not with α–β2 isozymes, whereas, in brain, it is only associated with α1–β isozymes. FXYD7 decreases the apparent K+ affinity of α1–β1 and α2–β1, but not of α3–β1 isozymes. These data suggest that FXYD7 is a novel, tissue‐ and isoform‐specific Na,K‐ATPase regulator which could play an important role in neuronal excitability.Keywords
This publication has 39 references indexed in Scilit:
- Differential Regulation of Renal Na,K-ATPase by Splice Variants of the γ SubunitPublished by Elsevier ,2002
- Functional Role and Immunocytochemical Localization of the γa and γb Forms of the Na,K-ATPase γ SubunitJournal of Biological Chemistry, 2001
- The FXYD Gene Family of Small Ion Transport Regulators or Channels: cDNA Sequence, Protein Signature Sequence, and ExpressionGenomics, 2000
- Role of β-Subunit Domains in the Assembly, Stable Expression, Intracellular Routing, and Functional Properties of Na,K-ATPaseJournal of Biological Chemistry, 1998
- Tissue-specific Distribution and Modulatory Role of the γ Subunit of the Na,K-ATPaseJournal of Biological Chemistry, 1997
- Oligomerization and maturation of Na,K-ATPase: functional interaction of the cytoplasmic NH2 terminus of the beta subunit with the alpha subunit.The Journal of cell biology, 1996
- Tissue-specific Versus Isoform-specific Differences in Cation Activation Kinetics of the Na,K-ATPaseJournal of Biological Chemistry, 1996
- Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na,K-ATPase.The Journal of cell biology, 1993
- Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ERCell, 1989
- Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the (sodium-potassium ion)-dependent ATPaseBiochemistry, 1978