Tau Phosphorylation

1. Tau Phosphorylation Tau is a highly soluble protein that mainly expressed in the neurons in the central nervous system (CNS), and it also distributes in glial cells such as oligodendrocytes and astrocytes in the CNS, as well as peripheral nervous system (PNS). Firstly discovered as a microtubule-associated protein (MAP) in 1975, Tau protein is primarily found in axons where it regulates microtubule polymerization and promotes microtubule stabilization. However, via the selective binding of diverse partners, Tau participates in multiple physiological processes including regulation of axonal diameter and growth, regulation of vesicle and organelle transport, modulation of signaling cascades by acting as a protein scaffold, cellular response to heat shock, adult neurogenesis and the establishment of neuronal polarity in development. Otherwise, abnormal Tau neurodegenerative diseases such as Alzheimer's disease (AD). functions are deeply involved in Tau protein is produced by alternative mRNA splicing of a single gene MAPT. Human MAPT is located at the chromosomal locus 17q21 and contains 16 exons, and alternative splicing of exons 2, 3, and 10 yields six isoforms. The structure of tau protein is divided into four regions: an acidic N-terminal region, a proline-rich region, a microtubule-binding domain (MBD) that is responsible for tau binding to microtubules and a C-terminal region. The MBD of Tau contains four repeat domains known as microtubule binding repeats R1, R2, R3 and R4, each of which contains a conserved consensus motif KXGS that can be phosphorylated at serine, resulting in the destabilization of the neuronal cytoskeleton. Find more: https://www.creative-diagnostics.com/tau-phosphorylation.htm