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Alzheimer's Protein Tau Researchers applied the STARFISH method to primary mouse neurons, detecting tau protein synthesis in dendrites, the branches that receive signals from other cells. A membrane-bound complex called the proteasome quickly degraded about a third of the new tau protein. When this complex was blocked in neurons and a mouse model with human tau, aggregates accumulated, depending on new protein synthesis. In a healthy brain, tau is mainly concentrated in axons, the long extensions through which a neuron transmits signals. In Alzheimer's disease, some tau appears in the cell body and dendrites, where protein clusters form. The authors asked if some of this protein is born directly in the dendrites. A map of mRNA shows where the cellular instructions for assembling a protein are located. STARFISH shows the moment when a ribosome reads the instructions and assembles the protein. In mouse neurons, the mRNA map of tau covered the cell body and extensions, while STARFISH detected active tau synthesis only in dendrites. A three-dimensional reconstruction separated the dendrites from intersecting axons. The authors labeled newly assembled tau for 30 seconds and tracked its fate, finding that almost half of the label disappeared within 30-60 seconds. The substance iBEp, which blocks the proteasome, stopped this rapid degradation, with the authors estimating that the proteasome degrades about a third of new tau. 🔗 Read original →