Graphical summary of Slc7a5 effects on Kvβ-mediated N-type inactivation. Schematic model depicting hypothetical orientations and interactions of Kv1.2 (gray), Kvβ (light blue), and Slc7a5 (green). The N-terminal ball-and-chain peptide of the Kvβ subunit, which confers N-type inactivation of Kv1.2, is depicted as a cartoon (black and blue) for visualization purposes. We observed that Slc7a5 promotes an interaction between Kv1.2 and Kvβ, and we propose that Slc7a5 primarily alters unbinding of the Kvβ inactivation peptide from the pore of Kv1.2, illustrated by the different relative rates in the colored boxes. The Kv1.2/Kvβ/Slc7a5 complex favors an inactivated state, reflected in a modest acceleration of inactivation and more prominently delayed recovery from inactivation compared with Kv1.2/Kvβ alone.