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Vol. 58, Issue 4, 677-683, October 2000
Department of Pharmacology (K.D.K., N.K., R.L.), Neuroscience
Graduate Program (R.L.), Penn State College of Medicine, Milton S. Hershey Medical Center, Hershey, Pennsylvania
We have generated a stable cell line expressing FLAG
epitope-tagged D3 dopamine receptors and used this cell line to study D3 receptor-protein interactions. To analyze protein interactions, we
separately introduced into the stable cell line either D3 receptors carrying an hemagglutinin (HA) epitope tag, or an HA-tagged version of
the D3 receptor splice variant D3nf. A combination of confocal laser
microscopy and coimmunoprecipitation was used to assay the formation
and expression pattern of D3-D3 homodimers or D3-D3nf heterodimers.
When coexpressed in HEK 293 cells, FLAG- and HA-tagged D3 receptors
exhibited a similar plasma membrane distribution. Using an HA epitope
tag-specific antibody, we coimmunoprecipitated HA- and FLAG-tagged D3
receptors, suggesting that D3 receptors are capable of forming
homodimers. Epitope-tagged D3nf polypeptides exhibited a markedly
different cellular distribution than D3 receptors. When expressed in
HEK 293 cells, either alone or in combination with FLAG-tagged D3
receptors, D3nf exhibited a punctate perinuclear distribution. When
D3nf was introduced into the stable D3-expressing cell line, D3
receptors were no longer visualized at the plasma membrane. Instead, D3
and D3nf showed a similar, predominantly cytosolic, localization. Using
the HA-specific antibody, we were able to coimmunoprecipitate D3 and
D3nf polypeptides from transfected cells. These data suggest the
existence of physical interaction between D3 and D3nf. This interaction
appears to result in the mislocalization of D3 receptors from the
plasma membrane to an intracellular compartment, a finding that could
be of significance in the etiology of schizophrenia.
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