Fig. 2
Inactivation of Kv1.1 is regulated by Kvβ and phosphorylation at S446. a Representative recordings, Isteady-state/Ipeak (Is/Ip), and peak current amplitudes of Kv1.1 with or without co-expression of Kvβ1.1 in HeLa cells. b Representative recordings and Is/Ip before and after the application of either IBMX/forskolin (I/F) or of the phorbol ester PMA. c Representative recordings, Is/Ip, and peak current amplitudes of the phosphorylation-deficient mutant Kv1.1S446A co-expressed with Kvβ1.1. d Representative recordings, Is/Ip, and peak current amplitudes of Kv1.1 after 1.5 h pre-incubation with a phosphatase inhibitor cocktail. *p < 0.05 (Student’s t test). e Left, Western blot with an anti-Kv1.1α antibody revealing phosphorylated and unphosphorylated Kv1.1α. At the bottom a longer exposure of the same blot is shown to demonstrate loss-of-phosphorylation when S446 was substituted by A. Protein levels of Kv1.1-S446A were consistently lower than of wild-type Kv1.1. Right, ratio of phosphorylated and unphosphorylated Kv1.1α, normalized to control conditions (n = 4 for control and I/F, n = 3 for PMA)