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A C‐terminally truncated human parathyroid hormone receptor is functional and activates multiple G proteins
Author(s) -
Schneider Helmut,
Feyen Jean H.M.,
Seuwen Klaus
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00878-7
Subject(s) - receptor , transfection , pertussis toxin , microbiology and biotechnology , hek 293 cells , 5 ht5a receptor , effector , chemistry , g protein coupled receptor , biology , g protein , biochemistry , gene
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 G i 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 G s