Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Gómez-Varela D,Barros F,Viloria CG,Giráldez T,Manso DG,Dupuy SG,Miranda P,de la Peña Pdoi
10.1016/s0014-5793(02)03888-7keywords:
subject
Has Abstractpub_date
2003-01-30 00:00:00pages
125-30issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302038887journal_volume
535pub_type
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