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Brain Protein Assembly Changes The study, published on July 30, tracked how age alters chemical marks on cysteine, an amino acid found in many proteins. In mice, this shift affected the function of synapsin-1 and G3BP2, and the H₂S donor accelerated the clearance of stress granules in cells. Proteins within cells constantly assemble into small, temporary clusters and then disassemble. This reversible assembly of proteins into droplets is called phase separation. The authors compared the frontotemporal region of the brain in mice at 10 weeks, 10 months, and 18 months. They measured two chemical states of cysteine: sulfenylation, where oxygen is added, and persulfidation, where a sulfur atom is added. With age, sulfenylation increased, while persulfidation decreased. Analysis of the total protein amount showed that this shift was not due to a change in the amount of the proteins themselves. The enzyme CSE produces H₂S and maintains persulfidation. In 10-week-old mice with the Cse gene knocked out, the cysteine oxidation profile already resembled that of 18-month-old animals. The team tracked the consequences on two proteins: synapsin-1, which organizes the reserve of neurotransmitter vesicles, and G3BP2, which assembles stress granules. In cells with CSE deficiency, such granules persisted longer after stress. In a purified system, H₂S dissolved pre-assembled G3BP2 condensates. In striatal cells, the slow-releasing H₂S donor GYY4137 accelerated granule clearance after oxidative stress, an effect also seen in fibroblasts from a 79-year-old donor, as reported in Nature Aging, July 2026. 🔗 Read original →