• Publications
  • Influence
Phospholemman (FXYD1) associates with Na,K-ATPase and regulates its transport properties
It is demonstrated 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 α-β isozymes of NKA after coexpression in Xenopus oocytes, and with α1–β, and less efficiently with α2–β iszymes, in native cardiac and skeletal muscles. Expand
Structure and mechanism of Na,K-ATPase: functional sites and their interactions.
Evidence is related on functional sites of Na,K-ATPase for the substrate (ATP), the essential cofactor (Mg(2+) ions), and the transported cations (Na(+) and K(+)) to the molecular structure to address the central questions of mechanism of active cation transport by all P-type cation pumps. Expand
Role of FXYD proteins in ion transport.
This review summarizes basic features of FXYD proteins and presents recent evidence for functional effects, structure-function relations and structural interactions with Na,K-ATPase, and considers evidence thatFXYD proteins affect functioning of other ion transport systems. Expand
Interaction with the Na,K-ATPase and Tissue Distribution of FXYD5 (Related to Ion Channel)*
FXYD5 (related to ion channel, dysadherin) is a member of the FXYD family of single span type I membrane proteins. Five members of this group have been shown to interact with the Na,K-ATPase and toExpand
Selectivity of Digitalis Glycosides for Isoforms of Human Na,K-ATPase*
Several digitalis glycosides, but not ouabain, are moderately α2-selective, which supports a major role of α2 in cardiac contraction and cardiotonic effects of digitalis Glycosides. Expand
Tissue-specific Distribution and Modulatory Role of the γ Subunit of the Na,K-ATPase
Evidence that the pig γ subunit, which migrates as a doublet on polyacrylamide gels, is sensitive to digestion by trypsin, and that Rb+ions partially protect it against this effect, indicate that the γSubunit is a tissue-specific regulator which shifts the steady-state equilibria toward E1. Expand
Functional Role and Immunocytochemical Localization of the γa and γb Forms of the Na,K-ATPase γ Subunit*
The importance of γa and γb may be related to their partially overlapping but distinct expression patterns and tissue-specific functions of the pump that these serve. Expand
Characterization of conformational changes in (Na,K) ATPase labeled with fluorescein at the active site
  • S. Karlish
  • Chemistry, Medicine
  • Journal of bioenergetics and biomembranes
  • 1 August 1980
The collected data support and extend the previous suggestion that K+ ions bound initially at a low-affinity site in state E1 are trapped in the occluded form E2· (K) by the conformational change poised far (Kc≈1000) in the direction of E2 · (K). Expand
The effect of membrane potential on the mammalian sodium‐potassium pump reconstituted into phospholipid vesicles.
Measurement of fluorescence changes of the carbocyanine dye DiS‐C3‐(5) showed that the ionophores generated potentials of the expected orientation and of sufficient stability for their effects on active transport to be assessed, demonstrating that values of diffusion potentials calculated from the Nernst or constant‐field equation are accurate. Expand
General and specific lipid-protein interactions in Na,K-ATPase.
The findings point to a central role of direct and specific interactions of different phospholipids and cholesterol in determining both stability and molecular activity of Na,K-ATPase and possible implications for physiological regulation by membrane lipid composition. Expand