G. Milligan

Diffusion and Oligomerization States of the Muscarinic M1 Receptor in Live Cells - The Impact of Ligands and Membrane Disruptors

This study uses single-molecule techniques to analyze the diffusion and oligomerization of M1R in live cells, showing ligands and membrane disruptors modulate these states.

Phosphorylation bar-coding of Free Fatty Acid receptor 2 is generated in a tissue-specific manner

The paper demonstrates tissue-specific phosphorylation patterns of FFA2 in response to the same agonist in different tissues using transgenic mice and phospho-specific antibodies.

Structural basis for the ligand recognition and signaling of free fatty acid receptors

The paper determines the structures of FFA1 and FFA4 bound to fatty acids and elucidates their activation mechanisms through cryo-EM and computational methods.

A new paradigm of intracrine free fatty acid receptor 4 signaling at lipid droplets

The paper shows FFA4, a GPCR, signals from lipid droplet-associated membranes in adipocytes, providing localized feedback to regulate lipolysis.

Phosphorylation of the M1 muscarinic acetylcholine receptor mediates protection in neurodegenerative disease

This study shows that phosphorylation and arrestin-dependent signaling of the M1 muscarinic receptor provides neuroprotection in prion disease, suggesting potential for developing safer therapies for neurodegenerative diseases.

Pathophysiological regulation of lung function by the free fatty acid receptor FFA4

This study shows that activating FFA4 reduces airway resistance in mouse models of inflammation and human lung tissue, suggesting it could be a therapeutic target for asthma and COPD.

Chemogenetic analysis of how receptors for short chain fatty acids regulate the gut-brain axis

This study identifies a specific agonist for a modified FFA2 receptor and demonstrates distinct roles of FFA2 and FFA3 in gut-brain communication using genetically engineered mice.

A general method to quantify ligand-driven oligomerization using single- or two-photon excitation microscopy

This paper introduces a method to quantify ligand-driven oligomerization using fluorescence intensity fluctuation spectrometry with single- or two-photon excitation microscopy, showing it can detect oligomer size and stability in membrane proteins.