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XB-ART-5815
FEBS Lett 2003 Jan 30;5351-3:125-30. doi: 10.1016/s0014-5793(02)03888-7.
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Relevance of the proximal domain in the amino-terminus of HERG channels for regulation by a phospholipase C-coupled hormone receptor.

Gómez-Varela D , Barros F , Viloria CG , Giráldez T , Manso DG , Dupuy SG , Miranda P , de la Peña P .


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We used Xenopus oocytes co-expressing thyrotropin-releasing hormone (TRH) receptors and human ether-a-go-go-related gene (HERG) K+ channel variants carrying different amino-terminal modifications to check the relevance of the proximal domain for hormonal regulation of the channel. Deletion of the whole proximal domain (Delta 138-373) eliminates TRH-induced modifications in activation and deactivation parameters. TRH effects on activation are also suppressed with channels lacking the second half of the proximal domain or only residues 326-373. However, normal responses to TRH are obtained with Delta 346-373 channels. Thus, whereas residues 326-345 are required for the hormonal modulation of HERG activation, different proximal domain sequences contribute to set HERG gating characteristics and its regulation by TRH.

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Species referenced: Xenopus
Genes referenced: kcnh2 trh