Abstract
The sodium-potassium ATPase (NKA) is the ion motive ATP-dependent transporter that establishes sodium and potassium gradients across the cell membrane, facilitating many physiological processes. In the heart, NKA activity is regulated by its interaction with phospholemman (PLM, FXYD1), a member of the FXYD protein family. PLM inhibits NKA by reducing pump’s apparent affinity of the pump for Na+, which is relieved by PLM phosphorylation. In this study, we used time-correlated single-photon counting, FRET-microscopy and molecular dynamics simulations to investigate the structure, stoichiometry, and affinity of the NKA-PLM regulatory complex.
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