For the phosphorylation state of microtubule-associated protein, tau plays a pivotal role in regulating microtubule networks in neurons. Tau promotes the assembly and stabilization of microtubules. The potential for tau to bind to microtubules is down-regulated after local phosphorylation. When we investigated the effects of PKN activation on tau phosphorylation, we found that PKN triggers disr...

Tau hyperphosphorylation can be considered as one of the hallmarks of Alzheimer's disease and other tauophaties. Besides its well-known role as a microtubule associated protein, Tau displays a key function as a protector of genomic integrity in stress situations. Phosphorylation has been proven to regulate multiple processes including nuclear translocation of Tau. In this contribution, we are a...

Background: Tau phosphorylation affects synaptic transmission, but the underlying mechanism remains elusive. Results: NMDA-receptor activation leads to phosphorylation of endogenous tau, thereby regulating the interaction of tau with Fyn and postsynaptic scaffolding protein PSD95. Conclusions: Phosphorylation of tau controls the interaction of tau with the postsynaptic PSD95/Fyn/NMDA-receptor c...

Phosphorylation of tau protein promotes stability of the axonal cytoskeleton; aberrant tau phosphorylation is implicated in the biogenesis of paired helical filaments (PHF) seen in Alzheimer's disease. Protein kinases and phosphatases that modulate tau phosphorylation have been identified using in vitro techniques; however, the role of these enzymes in vivo has not been determined. We used intr...

Abnormal phosphorylation and toxicity of a microtubule-associated protein tau are involved in the pathogenesis of Alzheimer's disease (AD); however, what pathological conditions trigger tau abnormality in AD is not fully understood. A reduction in the number of mitochondria in the axon has been implicated in AD. In this study, we investigated whether and how loss of axonal mitochondria promotes...

Hyperphosphorylation of Tau, a protein that stabilizes microtubules, leads to the breakdown of the microtubular structure and ultimately to the formation of neurofibrillar tangles within neurons. Here, we report monitoring of Tau phosphorylations electrochemically, using Tau protein films chemically linked to gold surfaces and 5'-γ-ferrocenyl (Fc) adenosine triphosphate (Fc-ATP) as a co-substra...

Glycogen synthase kinase 3beta (GSK3beta) phosphorylates substrates, including the microtubule-associated protein tau, at both primed and unprimed epitopes. GSK3beta phosphorylation of tau negatively regulates tau-microtubule interactions; however the differential effects of phosphorylation at primed and unprimed epitopes on tau is unknown. To examine the phosphorylation of tau at primed and un...

The microtubule-associated protein tau is hyperphosphorylated abnormally in AD and related neurodegenerative disorders. Many phospho epitopes created by proline directed kinases (SP/TP sites) show relative specificity for disease states. To test whether phosphorylation at the disease-associated SP/TP sites affects tau toxicity in vivo, we expressed a form of tau in Drosophila in which all SP/TP...

Tau is a protein that has received national mainstream recognition for its potential negative impact to the brain. This review succinctly provides information on structure of tau and normal physiological functions, including in hibernation changes throughout estrus cycle. There are many pathways involved phosphorylating diabetes, stroke, Alzheimer’s disease (AD), brain injury, aging, drug use. ...

Apoptosis has been characterized as a regulated, energy-dependent process. Specific protein-phosphorylation events have been demonstrated previously to occur during apoptosis and may play an important role in the regulation of this death process. In this study, energy metabolism and protein phosphorylation during apoptosis of neuronal PC12 cells induced by nerve growth factor and serum deprivat...