The carboxyl tail forms a discrete functional domain that blocks closure of the yeast K+ channel.
The carboxyl tail forms a discrete functional domain that blocks closure of the yeast K+ channel.
复制标题
羧基尾部形成一个离散的功能域，可阻止酵母 K 通道的关闭。
DOI：
10.1073/pnas.042538599
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发表时间：
2002
影响因子：
11.1
通讯作者：
Saimi,Yoshiro
中科院分区：
文献类型：
--
作者：
Loukin,StephenH;Lin,Junyu;Athar,Umair;Palmer,Christopher;Saimi,Yoshiro
Non-targeted mutagenesis studies of the yeast K+channel, TOK1, have led to identification of functional domains common to other cation channels as well as those so far not found in other channels. Among the latter is the ability of the carboxyl tail to prevent channel closure. Here, we show that the tail can fulfill this function intrans. Coexpression of the carboxyl tail with the tail-deleted channel core restores normal channel behavior.A Ser/Thr-rich region at its amino end and an acidic stretch at its carboxyl end delineate the minimal region required for tail function. This region of 160 aa apparently forms a discrete functional domain. Interaction of this domain with the channel core is strong, being recalcitrant to removal from excised membrane patches by both high salt and reducing agents. Although the use of a cytoplasmic domain to regulate channel is common among animal channels, by using it as a “foot-in-the-door” to maintain open state appears unique to TOK1, the first fungal K+channel studied in depth.
