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  • Title: Transmembrane peptide 4 and 5 of APJ are essential for its heterodimerization with OX1R.
    Author: Wan L, Xu F, Liu C, Ji B, Zhang R, Wang P, Wu F, Pan Y, Yang C, Wang C, Chen J.
    Journal: Biochem Biophys Res Commun; 2020 Jan 08; 521(2):408-413. PubMed ID: 31668922.
    Abstract:
    Increasing evidence indicates some G protein-coupled receptors function as a heterodimer, which provide a novel target for therapeutics investigation. However, study on the receptor-receptor interaction interface, a potent target on interfering dimer formation, are still limited. Here, using bioluminescence resonance energy transfer (BRET) combined with co-immunoprecipitation (Co-IP), we found a new constitutive GPCR heterodimer, apelin receptor (APJ)-orexin receptor type 1 (OX1R). Both APJ and OX1R co-internalized when constantly subjected to cognate agonist (apelin-13 or orexin-A) specific to either protomer. Combined with BRET and immunostaining, the in vitro synthesized transmembrane peptides (TMs) interfering experiments suggests that TM4 and 5 of APJ act as the interaction interface of the APJ-OX1R heterodimer, and co-internalization could be disrupted by these peptides as well. Our study not only provide new evidence on GPCR heterodimerization, but address a novel heterodimerization interface, which can be severed as a potential pharmacological target.
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