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J. Biol. Chem., Vol. 269, Issue 48, 30164-30172, Dec, 1994
MW Quick, MI Simon, N Davidson, HA Lester and AM Aragay
Xenopus oocytes were used to examine the coupling of the serotonin 1c
(5HT1c) and thyrotropin-releasing hormone (TRH) receptors to both
endogenous and heterologously expressed G protein alpha subunits.
Expression of either G protein-coupled receptor resulted in agonist-
induced, Ca(2+)-activated Cl- currents that were measured using a two-
electrode voltage clamp. 5HT-induced Cl- currents were reduced 80% by
incubating the injected oocytes with pertussis toxin (PTX) and inhibited
50-65% by injection of antisense oligonucleotides to the PTX- sensitive Go
alpha subunit. TRH-induced Cl- currents were reduced only 20% by PTX
treatment but were inhibited 60% by injection of antisense oligonucleotides
to the PTX-insensitive Gq alpha subunit. Injection of antisense
oligonucleotides to a novel Xenopus phospholipase C-beta inhibited the
5HT1c (and Go)-induced Cl- current with little effect on the TRH (and
Gq)-induced current. These results suggest that receptor- activated Go and
Gq interact with different effectors, most likely different isoforms of
phospholipase C-beta. Co-expression of each receptor with seven different
mammalian G protein alpha subunit cRNAs (Goa, Gob, Gq, G11, Gs, Golf, and
Gt) was also examined. Co-expression of either receptor with the first four
of these G alpha subunits resulted in a maximum 4-6-fold increase in Cl-
currents; the increase depended on the amount of G alpha subunit cRNA
injected. This increase was blocked by PTX for G alpha oa and G alpha ob
co-expression but not for G alpha q or G alpha 11 co-expression.
Co-expression of either receptor with Gs, Golf, or Gt had no effect on
Ca(2+)-activated Cl- currents; furthermore, co-expression with Gs or Golf
also failed to reveal 5HT- or TRH-induced changes in adenylyl cyclase as
assessed by activation of the cystic fibrosis transmembrane conductance
regulator Cl- channel. These results indicate that in oocytes, the 5HT1c
and TRH receptors do the following: 1) preferentially couple to
PTX-sensitive (Go) and PTX-insensitive (Gq) G proteins and that these G
proteins act on different effectors, 2) couple within the same cell type to
several different heterologously expressed G protein alpha subunits to
activate the oocyte's endogenous Cl- current, and 3) fail to couple to G
protein alpha subunits that activate cAMP or phosphodiesterase.
Differential coupling of G protein alpha subunits to seven-helix receptors expressed in Xenopus oocytes
Division of Biology, California Institute of Technology, Pasadena 91125.
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