Premium
Regulatory role of the extreme C‐terminal end of the S6 inner helix in C‐terminal‐truncated Kv1.2 channel activation
Author(s) -
Zhao LiLi,
Qi Zhi,
Zhang XianEn,
Bi LiJun,
Jin Gang
Publication year - 2010
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1042/cbi20090009
Subject(s) - terminal (telecommunication) , helix (gastropod) , channel (broadcasting) , c terminus , amino terminal , transmembrane domain , potassium channel , biophysics , amino acid , chemistry , biology , stereochemistry , genetics , peptide sequence , gene , telecommunications , computer science , ecology , snail
The transmembrane part of the S6 inner helix of the Kv1.2 potassium channel is a pivotal part in sustaining channel activity. However, the role of its extreme C‐terminal end, which is located on the cytoplasmic side of the channel, is largely unknown. Here, we investigated the role of the extreme C‐terminal end of the S6 inner helix (the HRET region) by constructing a series of C‐terminal‐truncated mutations related to this region in the C‐terminal‐truncated Kv1.2 channel. Mutations on Thr 421 or Glu 420 significantly altered the activation of the truncated channel. Mutations on Arg 419 demonstrated that neutral or basic, but not acidic amino acid, is essential at the position for the truncated channel activation, and no functional channel was observed when the channel was truncated from His 418 . Hence, our results indicate that the extreme C‐terminal end of the S6 inner helix plays an important regulatory role in the activation of the C‐terminal‐truncated Kv1.2 channel.