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Vol. 56, Issue 6, 1229-1237, December 1999
Department of Experimental Zoology, Utrecht University, Utrecht,
The Netherlands.
The gonadotropin-releasing hormone receptor (GnRH-R) of the African
catfish couples to phospholipase C and belongs to the large family of G
protein-coupled receptors. We recently demonstrated that removal of the
carboxyl-terminal tail (S331-Q379) from the catfish GnRH-R results in
a loss of agonist binding; the current study sought to define more
precisely the role of this region in receptor function. Progressive
truncations of the carboxyl-terminal tail decreased cell surface
expression detected by either enzyme-linked immunosorbent assay or
agonist-binding. The two most truncated receptors (stop331 and stop337)
showed no binding but were detected at the cell surface by
enzyme-linked immunosorbent assay. All receptors able to bind agonist
were also able to activate phospholipase C. The catfish GnRH-R was
phosphorylated after agonist-occupation and use of truncated mutants
showed this phosphorylation to be within the carboxyl-terminal tail.
Furthermore, studies with S356A, S363A and SS356,363AA mutant receptors
demonstrated that Ser363 is a major site of agonist-induced
phosphorylation. The absence of this phospho-acceptor site markedly
impaired agonist-mediated receptor internalization. In addition, both,
Ser363 and the last 12 residues of the tail (not containing Ser363)
were shown to be important for 
-arrestin-dependent internalization.
These observations are relevant to the regulatory function of the
carboxyl-terminal tail of G protein-coupled receptors in general and
are particularly intriguing given the absence of this region in
mammalian GnRH-Rs.
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