The current research in my lab concerns molecular and cellular aspects of the Na,K-ATPase (Sodium pump). The work includes studies aimed to define isoform- and tissue-specific diversity of the catalytic a subunit, in particular to gain insight into the question of whether and to what extent properties of the ubiquitous catalytic á1 subunit is modulated by interaction(s) with other proteins, namely members of the FXYD family of small transmembrane regulators. Another area of current interest concerns the role of cytoplasmic domains of the a subunit, which impact the mechanism of energy transduction between ATP binding, phosphorylation/dephosphorylation, conformational transitions and cation translocation.