Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A).

@article{Pfeiffer2001HomoAH,
  title={Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A).},
  author={Matthew Edwin Pfeiffer and Thomas Koch and Helmut Schr{\"o}der and Marcus Klutzny and Susanne Kirscht and Hans J{\"u}rgen Kreienkamp and Volker Hoellt and St. Schulz},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 17},
  pages={
          14027-36
        }
}
Several recent studies suggest that G protein-coupled receptors can assemble as heterodimers or hetero-oligomers with enhanced functional activity. However, inactivation of a fully functional receptor by heterodimerization has not been documented. Here we show that the somatostatin receptor (sst) subtypes sst(2A) and sst(3) exist as homodimers at the plasma membrane when expressed in human embryonic kidney 293 cells. Moreover, in coimmunoprecipitation studies using differentially epitope-tagged… CONTINUE READING
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