Overview:

The Tau families of proteins function to stabilize the microtubules by binding to them. Thus they have a key role in promoting the formation of microtubules and axons. Six Tau isoforms have been identified, which are produced by alternative splicing (1). Phosphorylaition of Tau proteins regulates their association with microtubules (2). Deposits of Alzheimer's disease AD-associated proteins, such as hyperphosphorylated Tau, as well as other shared misfolded proteins, such as, β-amyloid precursor protein (βAPP), ubiquitin, and various chaperones and protein kinases are thought to play a pathologic role in the cognitive decline and muscular failure. Malfunction of Tau proteins is associated with microtubules disintegration and collapsing of the neuronal transport system (3). Serine 416 is a target for phosphorylation in vitro by CaM kinase II (4).

References:

1. Goedert M. et al: Expression of separate isoforms of human tau protein: 2. Correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J 1990, 9, 4225-4230.3. Zilka, N., et al. Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo. FEBS Lett. 2006; 508: 3582-3588. 4. Rial, A. et al: Calcium Dyshomeostasis in β-Amyloid and Tau-bearing Skeletal Myotubes. J. Biol. Chem., 2004; 279: 3524-53532.