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Vol. 58, Issue 1, 120-128, July 2000
Departments of Pharmacology (S.P.L., B.F.O., G.V., S.R.G.),
Psychiatry (G.Y.N.), and Medicine (S.R.G.), University of Toronto,
Toronto, Ontario; Centre for Addiction and Mental Health (B.F.O., T.N.,
S.R.G.), Toronto, Ontario; and Mental Health Research Institute (H.A.,
A.M.), University of Michigan, Ann Arbor, Michigan
Numerous mutant G protein-coupled receptors with diminished or no
function have been described that are naturally occurring or that are
the product of gene manipulation. It has largely been assumed that
receptor mutants do not affect the function of the wild-type receptor;
however, the occurrence of G protein-coupled receptor dimerization
suggests the possibility that an intermolecular interaction between
mutant and wild-type receptors can occur. We have shown previously that
the D2 dopamine receptor (D2DR) exists as dimers in cell lines and
brain tissue. In this study, we demonstrated that mutant D2DR can
modulate the function of the wild-type D2DR. While attempting to
elucidate the structure of the D2DR dimer, we demonstrated that
nonfunctional D2DR substitution and truncation mutants antagonized
wild-type D2DR function. Furthermore, from analyses of this interaction
between the receptor mutants and the D2DR, using photoaffinity
labeling, we provide evidence that the D2DR is oligomeric in the cell.
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