Abstract
Proteins that interact with the human kappa opioid receptor (hKOPR) may contribute to regulation and signaling of the receptor. In this paper, we focus on the protein 14-3-3zeta that regulates anterograde transport of the hKOPR from the endoplasmic reticulum (ER) to the Golgi apparatus. 14-3-3zeta interacts with the C-terminal domain of the receptor and promotes cell surface expression of the hKOPR by inhibiting coatomer protein I (COPI) and RVR motif-mediated ER retension of the hKOPR. Here we describe three experimental procedures we used to evaluate the interaction between hKOPR and 14-3-3zeta: co-immunoprecipitation, pull-down assay and immunofluorescence microscopy.
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