Relevance of the proximal domain in the amino‐terminus of HERG channels for regulation by a phospholipase C‐coupled hormone receptor

FEBS Letters

Viloria, Cristina G¹  Manso, Diego G¹  Miranda, Pablo¹  Giráldez, Teresa¹  Gómez-Varela, David¹  de la Peña, Pilar¹  Barros, Francisco¹  Dupuy, Silvia G¹ 

[1] Departamento de Bioquı́mica y Biologı́a Molecular, Edificio Santiago Gascón, Campus del Cristo, Universidad de Oviedo, E-33006 Oviedo, Asturias, Spain

关键词: Human ether-a-go-go-related gene;    K+ channel;    Thyrotropin-releasing hormone receptor;    Hormonal regulation;    Gating;    Amino-terminus;    HERG;    human ether-a-go-go-related gene;    TRH;    thyrotropin-releasing hormone;    TRH-R;    TRH receptor;    PKC;    protein kinase C;    PKA;    protein kinase A;   

DOI  :  10.1016/S0014-5793(02)03888-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 (Δ138–373) 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 Δ346–373 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.

【 授权许可】

Unknown