Characterization of the Dimerization of Metabotropic Glutamate Receptors Using an N‐Terminal Truncation of mGluR1α

@article{Robbins1999CharacterizationOT,
  title={Characterization of the Dimerization of Metabotropic Glutamate Receptors Using an N‐Terminal Truncation of mGluR1$\alpha$},
  author={Melanie J. Robbins and Francisco Ciruela and Andrew D Rhodes and R. A. J. Mcilhinney},
  journal={Journal of Neurochemistry},
  year={1999},
  volume={72}
}
Abstract: The metabotropic glutamate receptor mGluR1α in membranes isolated both from rat brain and from cell lines transfected with cDNA coding for the receptor migrates as a disulphide‐bonded dimer on sodium dodecyl sulphate‐polyacrylamide gels. Dimerization of mGluR1α takes place in the endoplasmic reticulum because it is not prevented by exposing transfected human embryonic kidney (HEK) 293 cells to the drug brefeldin A, a drug that prevents egress of proteins from the endoplasmic reticulum… 
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    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
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