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J. Biol. Chem., Vol. 269, Issue 37, 23120-23127, Sep, 1994
SE Senogles
Site-directed mutations of the cDNA for Gi1 alpha, Gi21 alpha, and Gi3
alpha were constructed which changed the cysteine residue at the C terminus
to a glycine residue (Gi alpha PT). This mutation of the Gi alpha would not
permit the subsequent covalent modification by pertussis toxin, which
requires the cysteine moiety. The cDNA for each of the mutant Gi alpha
subunits was transfected into GH4C1 cells with either of the alternative
splice forms of the D2 dopamine receptor and clonal lines were generated.
After treatment with pertussis toxin to remove the contribution from
endogenous Gi proteins, the receptor- mediated inhibition of adenylyl
cyclase was examined. The D2 dopamine receptor, short form (D2s) signaled
through the Gi2 alpha PT mutant in these cells with an affinity for agonist
which was comparable to that observed in cells transfected with the cDNA
for D2s alone or the signaling observed in the absence of pertussis toxin.
The long form of the D2 dopamine receptor (D2l) signaled through the Gi3
alpha PT mutant to inhibit forskolin-stimulated adenylyl cyclase, with an
affinity for agonist comparable to that observed in cells transfected with
the cDNA for D2l alone. The receptor for somatostatin (somatotropin release
inhibiting factor) was used as an endogenous control receptor in these cell
lines. The somatotropin release inhibiting factor was able to signal
through both Gi1 alpha PT and Gi3 alpha PT to inhibit forskolin- stimulated
adenylyl cyclase. These results indicated that receptors use distinct Gi
proteins to signal to a common effector.
The D2 dopamine receptor isoforms signal through distinct Gi alpha proteins to inhibit adenylyl cyclase. A study with site-directed mutant Gi alpha proteins
Department of Biochemistry, University of Tennessee, Memphis 38163.
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