The Journal of Neuroscience, April 5, 2006, ():
Structural Determinants of M-Type KCNQ (Kv7) K+ Channel Assembly
J. Neurosci. Schwake et al.
26: 3757
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Supplementary figure legend
Homo- and heteromeric assembly of the KCNQ3(TD;Q1) construct.
Transfer of an N-glycosylation site within the extracellular "turret" domain (TD) from KCNQ1 into KCNQ3 was shown to result in strongly boosted expression of the resulting KCNQ3(TD;Q1) construct (Schenzer et al., 2005). Coiled-coil probability within the turret domain of KCNQ3 wild-type is shown in (A) and of KCNQ3(TD;Q1) in (B), each determined using the program Coils (Version 2.2). (C) and (D) probing for dominant negative effects of the pore mutants KCNQ1-G314S; KCNQ2-G279S, and KCNQ3-G318S on KCNQ2 currents. (C) Current-voltage relationships of KCNQ3(TD;Q1) (n = 25), KCNQ3(TD;Q1)+KCNQ1-G314S (n = 22), KCNQ3(TD;Q1)+KCNQ2-G279S (n = 19) and KCNQ3(TD;Q1) + KCNQ3-G318S) (n = 23). (D) Bar diagram of current levels obtained at the end of a 2 s-long voltage pulse to +40 mV. Currents from different oocyte batches were normalized to the mean KCNQ3(TD;Q1) current at +40mV.
