The large majority of studies into the structural basis for<unk>  modulation of Kv channels focus on its interaction with<unk>  (previously named KvLQT1). Residues in the transmembrane domain of<unk>  lies close to the selectivity filter of<unk>  within heteromeric<unk><unk>  channel complexes., The C-terminal domain of<unk> , specifically from amino acids 73 to 79 is necessary for stimulation of slow delayed potassium rectifier current by SGK1. The interaction of<unk>  with an alpha helix in the S6 KvLQT1 domain contributes to the higher affinity this channel has for benzodiazepine L7 and chromanol 293B by repositioning amino acid residues to allow for this.<unk>  destabilizes the S4-S5 alpha-helix linkage in the<unk>  channel protein in addition to destabilizing the S6 alpha helix, leading to slower activation of this channel when associated with<unk> . Variable stohiometries have been discussed but there are probably 2<unk>  subunits and 4<unk>  subunits in a plasma membrane IKs complex. The transmembrane segment of<unk>  is α-helical when in a membrane environment., The transmembrane segment of<unk>  has been suggested to interact with the<unk>  pore domain (S5/S6) and with the S4 domain of the<unk>  (KvLQT1) channel.<unk>  may bind to the outer part of the<unk>  pore domain, and slide from this position into the “activation cleft” which leads to greater current amplitudes<unk>  slows<unk>  activation several-fold, and there are ongoing discussions about the precise mechanisms underlying this. In a study in which<unk>  voltage sensor movement was monitored by site-directed fluorimetry and also by measuring the charge displacement associated with movement of charges within the S4 segment of the voltage sensor (gating current),<unk>  was found to slow S4 movement so much that the gating current was no longer measurable. Fluorimetry measurements indicated that<unk><unk>  channel S4 movement was 30-fold slower than that of the well-studied Drosophila Shaker Kv channel. Nakajo and Kubo found that<unk>  either slowed<unk>  S4 movement upon membrane depolarization, or altered S4 equilibrium at a given membrane potential. The Kass lab deduced that while homomeric<unk>  channels can open after the movement of a single S4 segment,<unk><unk>  channels can only open after all four S4 segments have been activated. The intracellular C-terminal domain of<unk>  is thought to sit on the<unk>  S4-S5 linker, a segment of<unk>  crucial for communicating S4 status to the pore and thus control activation.
KCNE1
MCN
CLCN1
AHDC1
PANO1
TAAR1
SLITRK1
SMN1