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Tuning of the Na,K-ATPase by the beta subunit

Scientific Reports2016Vol. 6(1), pp. 20442–20442

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Florian Hilbers, Wojciech Kopeć, Toke Jost Isaksen, Thomas Hellesøe Holm, Karin Lykke‐Hartmann, Poul Nissen, Himanshu Khandelia, Hanne Poulsen

Abstract

The vital gradients of Na(+) and K(+) across the plasma membrane of animal cells are maintained by the Na,K-ATPase, an αβ enzyme complex, whose α subunit carries out the ion transport and ATP hydrolysis. The specific roles of the β subunit isoforms are less clear, though β2 is essential for motor physiology in mammals. Here, we show that compared to β1 and β3, β2 stabilizes the Na(+)-occluded E1P state relative to the outward-open E2P state, and that the effect is mediated by its transmembrane domain. Molecular dynamics simulations further demonstrate that the tilt angle of the β transmembrane helix correlates with its functional effect, suggesting that the relative orientation of β modulates ion binding at the α subunit. β2 is primarily expressed in granule neurons and glomeruli in the cerebellum, and we propose that its unique functional characteristics are important to respond appropriately to the cerebellar Na(+) and K(+) gradients.

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Abstract

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