TYK2 inhibition may offer new strategy to reduce tau toxicity in Alzheimer's

Alzheimer's Disease News

TYK2 inhibition may offer new strategy to reduce tau toxicity in Alzheimer's
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Researchers at Baylor College of Medicine, the Jan and Dan Duncan Neurological Research Institute (Duncan NRI) at Texas Children's Hospital and collaborating institutions discovered that the enzyme TYK2 transforms the normal protein tau into one that accumulates in the brain and contributes to the development of Alzheimer's disease in animal...

Baylor College of Medicine Nov 12 2024 Research ers at Baylor College of Medicine , the Jan and Dan Duncan Neurological Research Institute at Texas Children 's Hospital and collaborating institutions discovered that the enzyme TYK2 transforms the normal protein tau into one that accumulates in the brain and contributes to the development of Alzheimer's disease in animal models.

Previous studies showed that tau is chemically modified in disease, predominantly by the addition of extra phosphate to the Tyrosine groups in the protein, and that these changes play a crucial role in regulating tau accumulation. Working with human cells and animal models of tau-driven dementia, the researchers are the first to show that TYK2's modifications to tau contribute to tau-mediated disease. "We found that TYK2 adds phosphate groups to tau at a particular location on the protein identified as Tyrosine 29," Kim said. "This modification stabilizes tau levels in human cells and mouse neurons by making it resistant to autophagy, a cellular process important for clearing proteins," Kim said.

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