A C-terminally truncated human parathyroid hormone receptor is functional and activates multiple G proteins.
FEBS Lett
; 351(2): 281-5, 1994 Sep 05.
Article
em En
| MEDLINE
| ID: mdl-8082781
ABSTRACT
We have investigated the role of the C-terminal cytoplasmic domain of the human PTH receptor in effector coupling. Following transient expression in COS-1 cells, coupling to both AC and PI-PLC was observed with the full-length receptor. Progressive C-terminal truncations did not dissociate activation of the two signalling systems. In stably transfected 293 cells, however, the full-length receptor as well as the majority of truncated constructs stimulated AC exclusively but failed to activate PI-PLC. Activation of both signalling systems was again observed following stable expression of a severely truncated receptor (R483) in 293 cells. In this case, pertussis toxin was also found to potentiate the cAMP response to hPTH-(1-38) significantly, indicating functional coupling of R483 to Gi proteins. Our results suggest that a core region of the human PTH receptor (first, second, third intracellular loop) can interact promiscuously with different G proteins and that the C-terminus of the full-length receptor directs the receptor towards an interaction with Gs.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Hormônio Paratireóideo
/
Transdução de Sinais
/
Receptores de Hormônios Paratireóideos
/
Proteínas de Ligação ao GTP
Limite:
Humans
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1994
Tipo de documento:
Article