![]() In addition, phosphorylation of Tau repeats promotes liquid–liquid phase separation at cellular protein conditions. ![]() Alternative splicing of Tau can thus regulate the formation of Tau-containing membrane-less compartments. Furthermore, we demonstrate that three-repeat and four-repeat isoforms of Tau differ in their ability for demixing. Liquid–liquid demixing causes molecular crowding of amyloid-promoting elements of Tau and drives electrostatic coacervation. Here, we show that the microtubule-binding repeats of Tau, which are lysine-rich, undergo liquid–liquid phase separation in solution. It is still unclear what initiates the conversion from an innocuous phase of high solubility and functionality to solid-like neurotoxic deposits. ![]() In solution, however, Tau is intrinsically disordered, highly soluble, and binds to microtubules. The protein Tau aggregates into tangles in the brain of patients with Alzheimer’s disease.
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