Charybdotoxin binding in the I(Ks) pore demonstrates two MinK subunits in each channel complex.

Abstract:

:I(Ks) voltage-gated K(+) channels contain four pore-forming KCNQ1 subunits and MinK accessory subunits in a number that has been controversial. Here, I(Ks) channels assembled naturally by monomer subunits are compared to those with linked subunits that force defined stoichiometries. Two strategies that exploit charybdotoxin (CTX)-sensitive subunit variants are applied. First, CTX on rate, off rate, and equilibrium affinity are found to be the same for channels of monomers and those with a fixed 2:4 MinK:KCNQ1 valence. Second, 3H-CTX and an antibody are used to directly quantify channels and MinK subunits, respectively, showing 1.97 +/- 0.07 MinK per I(Ks) channel. Additional MinK subunits do not enter channels of monomeric subunits or those with fixed 2:4 valence. We conclude that two MinK subunits are necessary, sufficient, and the norm in I(Ks) channels. This stoichiometry is expected for other K(+) channels that contain MinK or MinK-related peptides (MiRPs).

journal_name

Neuron

journal_title

Neuron

authors

Chen H,Kim LA,Rajan S,Xu S,Goldstein SA

doi

10.1016/s0896-6273(03)00570-1

subject

Has Abstract

pub_date

2003-09-25 00:00:00

pages

15-23

issue

1

eissn

0896-6273

issn

1097-4199

pii

S0896627303005701

journal_volume

40

pub_type

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