
Fat Chat
Native mass spectrometry reveals how lipids and proteins communicate at cell membranes
Charlotte Barker |
By visualizing molecular interactions in the cell membrane with a pioneering mass spectrometry (MS) method, researchers at Texas A&M University have shown how proteins are able to recruit a specific lipid microenvironment via allostery (1). A common feedback mechanism in biology, allostery is the regulation or modulation of a biological macromolecule through the binding of an effector ligand to a binding site other than the active site.
The Texas researchers have shown that this method of communication extends to lipids. When monitoring individual lipid binding with native ion mobility MS – a technique pioneered by group leader Arthur Laganowsky that preserves non-covalent interactions – the group noted that different lipid pairs exhibit various degrees of allosteric modulation.
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