In addition to providing energy, lipids are also essential building blocks of our cell membranes. However, despite their importance, they remain poorly understood. A team from the University of Geneva (UNIGE) has revealed for the first time the secrets of their transport within cells. Each lipid uses a limited number of proteins to move from its place of production to its place of action. The team has also compiled an inventory of the proteins involved in the transport of hundreds of lipids. These findings, published in the journal Nature, provide a better picture of the functioning of our cells, as well as of many genetic and metabolic disorders, such as diabetes and Alzheimer's disease.

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A new analysis has elucidated the structure and activation mechanisms of the human receptor HCAR1, which is involved in many metabolic and inflammatory conditions. By teasing apart the mechanisms of the receptor’s activation, the findings could inform research into therapies that target HCAR1. This receptor is found in fat, neurons, skeletal muscle, and other tissue types, and fills various roles in metabolism and in reducing inflammation. The receptor’s wide-ranging functions suggest that it could be a solid target in cancer and stroke, as well as in neurodegenerative conditions such as Alzheimer’s disease. However, there are still no potent activators or inhibitors of HCAR1, and scientists know little about how the receptor recognizes its binding partners and becomes activated. Here, Mengru Gao and colleagues harnessed cryo-electron microscopy to interrogate the structure and function of HCAR1 in complex with the G protein subunit Gα_i1. They studied HCAR1 in its unbound state and when it was bound to either lactate – its normal metabolite ligand – or a synthetic activator named CHBA. The authors found that HCAR1 had a smaller and more compact ligand-binding pocket compared with those of other HCARs, such as HCAR2. Lactate bound fairly weakly to HCAR1 and only activated the receptor at relatively high concentrations, but CHBA was more potent and bound more stably. Further research revealed that HCAR1 became self-activated through structural rearrangement of its extracellular loop 2 region. “This study fills gaps in our knowledge of the structure of HCAR1 and elucidates the differences between self-activation and ligand-dependent activation of the receptor, potentially providing a structural and theoretical basis for the design of inverse, selective, and high-efficiency agonists,” the authors conclude.

A groundbreaking international study has demonstrated that Alzheimer's disease biomarkers can be accurately detected using simple finger-prick blood samples that can be collected at home and mailed to laboratories without refrigeration or prior processing.