Different combinations of insect Na,K-ATPase α- and β-subunits enable fine-tuned adaptation to host plant toxins and tissue specific needs

Marlena Winter, Safaa Dalla, Vera Wagschal, Rohin Turjalei, Marlies Heiser & Susanne Dobler
Background Cardiac glycosides are known to fatally inhibit the Na,K-ATPase throughout the animal kingdom. Several animals, however, evolved target-site insensitivity by substitutions in the otherwise highly conserved cardiac glycoside binding pocket located on the Na,K-ATPase α-subunit. The minimal functional enzyme consist of an α- and a β-subunit, the latter considered mainly as a chaperone responsible for correct folding and membrane integration. We here analyze resistance to cardiac glycosides and kinetic properties of different Na,K-ATPase α/β-combinations...
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