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Heterodimerization of mu opioid receptor protomer with dopamine D2 receptor modulates agonist-induced internalization of mu opioid receptor

Lakshmi Vasudevan, Dasiel O Borroto-Escuela, Jelle Huysentruyt (UGent) , Kjell Fuxe, Deepak K Saini and Christophe Stove (UGent)
(2019) BIOMOLECULES. 9(8).
Author
Organization
Abstract
The interplay between the dopamine (DA) and opioid systems in the brain is known to modulate the additive effects of substances of abuse. On one hand, opioids serve mankind by their analgesic properties, which are mediated via the mu opioid receptor (MOR), a Class A G protein-coupled receptor (GPCR), but on the other hand, they pose a potential threat by causing undesired side effects such as tolerance and dependence, for which the exact molecular mechanism is still unknown. Using human embryonic kidney 293T (HEK 293T) and HeLa cells transfected with MOR and the dopamine D-2 receptor (D2R), we demonstrate that these receptors heterodimerize, using an array of biochemical and biophysical techniques such as coimmunoprecipitation (co-IP), bioluminescence resonance energy transfer (BRET1), F0rster resonance energy transfer (FRET), and functional complementation of a split luciferase. Furthermore, live cell imaging revealed that D2LR, when coexpressed with MOR, slowed down internalization of MOR, following activation with the MOR agonist [D-Ala2, N-MePhe4, Gly-ol]-enkephalin (DAMGO).
Keywords
G protein-coupled receptor, heterodimerization, mu opioid receptor, dopamine D-2 receptor, PROTEIN-COUPLED RECEPTORS, BETA-ARRESTIN 2, MORPHINE-TOLERANCE, GPCR DIMERIZATION, DESENSITIZATION, OLIGOMERIZATION, MECHANISMS, PHOSPHORYLATION, ANALGESIA, OPIATE

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Citation

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MLA
Vasudevan, Lakshmi, et al. “Heterodimerization of Mu Opioid Receptor Protomer with Dopamine D2 Receptor Modulates Agonist-Induced Internalization of Mu Opioid Receptor.” BIOMOLECULES, vol. 9, no. 8, 2019, doi:10.3390/biom9080368.
APA
Vasudevan, L., Borroto-Escuela, D. O., Huysentruyt, J., Fuxe, K., Saini, D. K., & Stove, C. (2019). Heterodimerization of mu opioid receptor protomer with dopamine D2 receptor modulates agonist-induced internalization of mu opioid receptor. BIOMOLECULES, 9(8). https://doi.org/10.3390/biom9080368
Chicago author-date
Vasudevan, Lakshmi, Dasiel O Borroto-Escuela, Jelle Huysentruyt, Kjell Fuxe, Deepak K Saini, and Christophe Stove. 2019. “Heterodimerization of Mu Opioid Receptor Protomer with Dopamine D2 Receptor Modulates Agonist-Induced Internalization of Mu Opioid Receptor.” BIOMOLECULES 9 (8). https://doi.org/10.3390/biom9080368.
Chicago author-date (all authors)
Vasudevan, Lakshmi, Dasiel O Borroto-Escuela, Jelle Huysentruyt, Kjell Fuxe, Deepak K Saini, and Christophe Stove. 2019. “Heterodimerization of Mu Opioid Receptor Protomer with Dopamine D2 Receptor Modulates Agonist-Induced Internalization of Mu Opioid Receptor.” BIOMOLECULES 9 (8). doi:10.3390/biom9080368.
Vancouver
1.
Vasudevan L, Borroto-Escuela DO, Huysentruyt J, Fuxe K, Saini DK, Stove C. Heterodimerization of mu opioid receptor protomer with dopamine D2 receptor modulates agonist-induced internalization of mu opioid receptor. BIOMOLECULES. 2019;9(8).
IEEE
[1]
L. Vasudevan, D. O. Borroto-Escuela, J. Huysentruyt, K. Fuxe, D. K. Saini, and C. Stove, “Heterodimerization of mu opioid receptor protomer with dopamine D2 receptor modulates agonist-induced internalization of mu opioid receptor,” BIOMOLECULES, vol. 9, no. 8, 2019.
@article{8635909,
  abstract     = {{The interplay between the dopamine (DA) and opioid systems in the brain is known to modulate the additive effects of substances of abuse. On one hand, opioids serve mankind by their analgesic properties, which are mediated via the mu opioid receptor (MOR), a Class A G protein-coupled receptor (GPCR), but on the other hand, they pose a potential threat by causing undesired side effects such as tolerance and dependence, for which the exact molecular mechanism is still unknown. Using human embryonic kidney 293T (HEK 293T) and HeLa cells transfected with MOR and the dopamine D-2 receptor (D2R), we demonstrate that these receptors heterodimerize, using an array of biochemical and biophysical techniques such as coimmunoprecipitation (co-IP), bioluminescence resonance energy transfer (BRET1), F0rster resonance energy transfer (FRET), and functional complementation of a split luciferase. Furthermore, live cell imaging revealed that D2LR, when coexpressed with MOR, slowed down internalization of MOR, following activation with the MOR agonist [D-Ala2, N-MePhe4, Gly-ol]-enkephalin (DAMGO).}},
  articleno    = {{368}},
  author       = {{Vasudevan, Lakshmi and Borroto-Escuela, Dasiel O and Huysentruyt, Jelle and Fuxe, Kjell and Saini, Deepak K and Stove, Christophe}},
  issn         = {{2218-273X}},
  journal      = {{BIOMOLECULES}},
  keywords     = {{G protein-coupled receptor,heterodimerization,mu opioid receptor,dopamine D-2 receptor,PROTEIN-COUPLED RECEPTORS,BETA-ARRESTIN 2,MORPHINE-TOLERANCE,GPCR DIMERIZATION,DESENSITIZATION,OLIGOMERIZATION,MECHANISMS,PHOSPHORYLATION,ANALGESIA,OPIATE}},
  language     = {{eng}},
  number       = {{8}},
  pages        = {{17}},
  title        = {{Heterodimerization of mu opioid receptor protomer with dopamine D2 receptor modulates agonist-induced internalization of mu opioid receptor}},
  url          = {{http://dx.doi.org/10.3390/biom9080368}},
  volume       = {{9}},
  year         = {{2019}},
}
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