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Integrated structural modeling and super-resolution imaging resolve GPCR oligomers.

Francesca Fanelli1, Aylin C Hanyaloglu2, Kim Jonas3

  • 1Department Life Sciences, University of Modena and Reggio Emilia, Modena, Italy; Center for Neuroscience and Neurotechnology, University of Modena and Reggio Emilia, Modena, Italy.

Progress in Molecular Biology and Translational Science
|January 19, 2020
PubMed
Summary

G protein-coupled receptors (GPCRs) form dimers and oligomers that regulate signaling. Studying the luteinizing hormone receptor (LHR) using advanced imaging and modeling reveals its complex oligomeric structures and interfaces.

Keywords:
DimerGlycoprotein hormone receptorsLuteinizing hormone receptorMolecular modelingMolecular recognitionProtein-protein dockingSignalingSuper-resolution imaging

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • G protein-coupled receptors (GPCRs) form dimers and oligomers, crucial for their signaling.
  • The function of individual protomers within GPCR oligomers is not fully understood.
  • Glycoprotein hormone receptors (GpHRs), a Class A/rhodopsin subfamily, are known to be regulated by oligomerization in health and disease.

Purpose of the Study:

  • To elucidate the structural organization and functional implications of GPCR oligomerization.
  • To investigate the role of the luteinizing hormone receptor (LHR) in GPCR oligomerization.
  • To combine atomistic modeling with super-resolution imaging to understand LHR assembly.

Main Methods:

  • Utilized protein-protein docking for atomistic modeling of GPCR complexes.
  • Employed photoactivated dual-color localization microscopy (PD-PALM) for super-resolution imaging of single LHR molecules.
  • Resolved LHR structures at approximately 8nm resolution, identifying functional asymmetric dimers and oligomers.

Main Results:

  • Demonstrated functional asymmetric dimers and higher-order oligomers of the LHR.
  • Structural modeling of LHR trimers and tetramers showed strong alignment with imaging data.
  • Identified multiple helix interfaces involved in inter-protomer associations within LHR oligomers.

Conclusions:

  • GPCR oligomerization, particularly of LHR, involves diverse spatial and structural assemblies.
  • These assemblies can acutely fine-tune cellular signaling profiles.
  • Understanding GPCR oligomerization is key to comprehending their roles in physiological and pathophysiological processes.