Dimerization of the melanocortin 4 receptor: A study using bioluminescence resonance energy transfer

The melanocortin 4 receptor is important in the regulation of satiety. In this study we have investigated the propensity of the MC4 receptor to homodimerize. MC4 receptors with either a modified green fluorescent protein (GFP 2) or Renilla luciferase (RLuc) at their C-terminus were constructed. Thes...

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Veröffentlicht in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2006-02, Vol.27 (2), p.380-387
Hauptverfasser: Nickolls, Sarah A., Maki, Rich A.
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Maki, Rich A.
description The melanocortin 4 receptor is important in the regulation of satiety. In this study we have investigated the propensity of the MC4 receptor to homodimerize. MC4 receptors with either a modified green fluorescent protein (GFP 2) or Renilla luciferase (RLuc) at their C-terminus were constructed. These receptors showed equivalent binding and functional properties to the wild-type MC4 receptor. Bioluminescence resonance energy transfer readings indicated that the MC4 receptor exists as a constitutive homodimer, which was not regulated by peptide interaction. The efficiency of MC4 receptor to form homodimers was greatly enhanced compared to its ability to heterodimerize with the kappa opioid receptor.
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ispartof Peptides (New York, N.Y. : 1980), 2006-02, Vol.27 (2), p.380-387
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1873-5169
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source MEDLINE; Elsevier ScienceDirect Journals Complete
subjects BRET
Cell Line
Dimerization
Fluorescence Resonance Energy Transfer
G protein coupled receptor
Green Fluorescent Proteins - agonists
Green Fluorescent Proteins - genetics
Humans
Ligands
Luminescence
MC4R
Melanocortin
Protein Structure, Secondary
Receptor, Melanocortin, Type 4 - agonists
Receptor, Melanocortin, Type 4 - genetics
Receptor, Melanocortin, Type 4 - metabolism
Receptors, Opioid, kappa - metabolism
title Dimerization of the melanocortin 4 receptor: A study using bioluminescence resonance energy transfer
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