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Abstract
Tau protein is abundant in the central nervous system and involved in microtubule assembly and stabilization. It is predominantly associated with axonal microtubules and present at lower level in dendrites where it is engaged in signaling functions. Post-translational modifications of tau and its interaction with several proteins play an important regulatory role in the physiology of tau. As a consequence of abnormal modifications and expression, tau is redistributed from neuronal processes to the soma and forms toxic oligomers or aggregated deposits. The accumulation of tau protein is increasingly recognized as the neuropathological hallmark of a number of dementia disorders known as tauopathies. Dysfunction of tau protein may contribute to collapse of cytoskeleton, thereby causing improper anterograde and retrograde movement of motor proteins and their cargos on microtubules. These disturbances in intraneuronal signaling may compromise synaptic transmission as well as trophic support mechanisms in neurons.
Highlights
Tau protein belongs to the family of natively unfolded microtubule-associated proteins that binds to microtubules, is involved in their assembly and stabilization [1] and in regulation of the motor-driven axonal transport
Kinases which are involved in tau phosphorylation can be divided into three classes: proline-directed protein kinases (PDPK), non-PDPK protein kinases and tyrosine protein kinases (TPK)
Tau protein kinase I (TPKI) is a non-PDPK that can phosphorylate native tau isolated from normal brain, which is already phosphorylated to some extent, but it can not phosphorylate completely dephosphorylated tau
Summary
Tau protein belongs to the family of natively unfolded microtubule-associated proteins that binds to microtubules, is involved in their assembly and stabilization [1] and in regulation of the motor-driven axonal transport. Phosphorylated tau accumulates in the somatodendritic compartment of neurons, aggregates and eventually forms neurofibrillary tangles (NFTs) [13]. It has been shown that highly phosphorylated tau interferes with neuronal functions, such as mitochondrial respiration and axonal transport [15,16]. Tau excessive phosphorylation and aggregation could be driven by its interaction with several other proteins like β-amyloid, Fyn kinase, Pin, heat shock cognate Hsc and heat shock protein Hsp, immunophilins FKBP51 and FKBP52, α-synuklein or actin interacting protein PACSIN1. As the consequence of these interactions tau accumulates in dendritic spines, where it suppresses synaptic responses [17,18]. In neurons excessively phosphorylated tau is involved in: microtubule destabilization, impaired axonal transport of substances [19], post-synaptic dysfunction, compromised cell signaling and, as consequence, cognitive impairments ensue [20]
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