The article discusses the emerging roles of lipids in shaping the function of membrane proteins. It highlights the direct link between the lipid environment and the structure and function of membrane proteins, emphasizing that lipid-induced perturbations to the membrane shape can significantly influence protein function. The authors use models and experiments to demonstrate that the lipid bilayer is not a passive bystander but plays an essential role in determining the function of membrane-bound proteins. They focus on mechanosensitive channels as a case study, showing how the physicochemical properties of the lipid bilayer affect channel function. The article also explores the influence of membrane doping and the effects of membrane mechanics on protein function, particularly in the context of hydrophobic mismatch and membrane tension. The authors propose that the lipid environment can be used to dissect the structure-function relationship of membrane proteins and suggest further exploration of membrane crowding and its impact on protein interactions.The article discusses the emerging roles of lipids in shaping the function of membrane proteins. It highlights the direct link between the lipid environment and the structure and function of membrane proteins, emphasizing that lipid-induced perturbations to the membrane shape can significantly influence protein function. The authors use models and experiments to demonstrate that the lipid bilayer is not a passive bystander but plays an essential role in determining the function of membrane-bound proteins. They focus on mechanosensitive channels as a case study, showing how the physicochemical properties of the lipid bilayer affect channel function. The article also explores the influence of membrane doping and the effects of membrane mechanics on protein function, particularly in the context of hydrophobic mismatch and membrane tension. The authors propose that the lipid environment can be used to dissect the structure-function relationship of membrane proteins and suggest further exploration of membrane crowding and its impact on protein interactions.