![]() This inhibits tau’s ability to stimulate microtubule assembly and promotes self-aggregation, like abnormally hyperphosphorylated tau in AD brainġ3. ![]() DYRK1A was shown to phosphorylate microtubule-associated protein tau at T212 to prime tau for subsequent phosphorylation by GSK-3β at S308ġ3. The level of DYRK1A is elevated in a gene dosage-dependent manner in DS, suggesting that the protein not only plays an important role in regulating normal brain functions, but also in the etiology of DSĭYRK1A has been linked to neurofibrillary degeneration and β-amyloidosis of ADġ1. ![]() DYRK1A in the brain displays a distinct structure-specific distribution patternĨ, and it interacts with an array of factors involved in neuronal development, proliferation, and differentiationĩ. Transgenic mice carrying an extra copy of DYRK1A have been shown to exhibit symptoms similar to DS, including brain abnormalities, neurodevelopmental delay, and memory impairmentsħ. Almost all DS cases inevitably lead to the development of Alzheimer’s disease (AD)-type pathologyĤ. DS, the most common chromosomal abnormality associated with birth defects and developmental disabilities, is caused by full or partial trisomy of chromosome 21ģ. 1 is mapped to a region of chromosome 21 implicated in Down syndrome (DS)Ģ. ![]()
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