The N-terminus of the Na+,K+-ATPase α-subunit shows some homology to that of Shaker-B K+ channels; the latter has been shown to mediate the N-type channel inactivation in a ball-and-chain mechanism. When the Torpedo Na+,K+-ATPase is expressed in Xenopus oocytes and the pump is transformed into an ion channel with palytoxin (PTX), the channel exhibits a time-dependent inactivation gating at positive potentials. The inactivation gating is eliminated when the N-terminus is truncated by deleting the first 35 amino acids after the initial methionine. The inactivation gating is restored when a synthetic N-terminal peptide is applied to the truncated pumps at the intracellular surface. Truncated pumps generate no electrogenic current and exhibit an altered stoichiometry for active transport. Thus, the N-terminus of the α-subunit appears to act like an inactivation gate and performs a critical step in the Na+,K+-ATPase pumping function. © 2002 Elsevier Science B.V. All rights reserved.
Wu, C. H., Vasilets, L. A., Takeda, K., Kawamura, M., & Schwarz, W. (2003). Functional role of the N-terminus of Na+,K+-ATPase α-subunit as an inactivation gate of palytoxin-induced pump channel. Biochimica et Biophysica Acta - Biomembranes, 1609(1), 55–62. https://doi.org/10.1016/S0005-2736(02)00653-3