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Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

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Conformational pathway provides unique sensitivity to a synaptic mGluR.

Chris H Habrian¹, Joshua Levitz^2,3, Vojtech Vyklicky²

¹Biophysics Graduate Group, University of California, Berkeley, CA, 94720, USA.

Nature Communications

|December 6, 2019

Summary

Metabotropic glutamate receptors (mGluRs) function at synapses. The mGluR2/7 heterodimer exhibits high affinity and efficacy, enabling it to detect glutamate signals from both nearby and distant synapses.

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Area of Science:

Neuroscience
Molecular Biology
Biochemistry

Background:

Metabotropic glutamate receptors (mGluRs) are crucial G-protein-coupled receptors in synaptic function.
The mGluR7 homodimer displays low affinity and efficacy, suggesting it's insufficient for synaptic activation.

Purpose of the Study:

To investigate the functional properties of mGluR7, particularly its heterodimerization with mGluR2.
To elucidate the activation mechanisms and synaptic responsiveness of the mGluR2/7 heterodimer.

Main Methods:

Utilized macroscopic and single-molecule Förster Resonance Energy Transfer (FRET) to monitor structural changes.
Assessed receptor affinity, efficacy, and cooperativity in the mGluR2/7 heterodimer.

Main Results:

The mGluR7 homodimer has a significantly lower affinity and maximal activation compared to other mGluRs.
The mGluR2/7 heterodimer demonstrates high affinity and efficacy, with cooperative activation.
mGluR2/7 exhibits a unique activation pathway, showing partial activation even in the Apo state with antagonists bound.

Conclusions:

The mGluR2/7 heterodimer possesses high sensitivity and a broad dynamic range, suitable for detecting diverse glutamate signaling.
Heterodimerization with mGluR2 rescues the functional limitations of mGluR7, enabling its role in synaptic transmission.