"Phosphorylation of The Tau Protein in Neurodegenerative Disease"

Abstract

Protein phosphorylation is a reversible post-translational modification that involves a series of sequence-specific kinases and occurs on specific residues such as serine, threonine, and tyrosine. The reversible phosphorylation of proteins regulates almost all aspects of the cell's life cycle and abnormal phosphorylation is the cause or consequence of many diseases. Protein phosphorylation states can mediate protein complex formation and regulate protein function, which is important for cell physiology but can also promote neuropathic events. The tau protein is a very important microtubule-associated protein in the brain, occurring most commonly in neurons and glial cells. Its level of phosphorylation is associated with a variety of diseases of the central nervous system such as Alzheimer's disease. Under normal circumstances, post-transcriptional tau phosphorylation is conducive to the stability of microtubules. However, hyperphosphorylation can lead to the deformation and aggregation of various types of cytoskeletal components of nerve tissue, causing them to lose normal function.