Glycosylation of microtubule-associated protein tau in Alzheimer's disease brain

1999 ◽  
Vol 97 (6) ◽  
pp. 635-641 ◽  
Author(s):  
M. Takahashi ◽  
Yasumi Tsujioka ◽  
Tatsuo Yamada ◽  
Yoshio Tsuboi ◽  
Hidechika Okada ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Tau ◽  
Microtubule Associated Protein Tau

Interaction of 14-3-3ζ with Microtubule-Associated Protein Tau within Alzheimer’s Disease Neurofibrillary Tangles

Biochemistry ◽  
2013 ◽  
Vol 52 (37) ◽  
pp. 6445-6455 ◽  
Author(s):  
Hamid Y. Qureshi ◽  
Tong Li ◽  
Ryen MacDonald ◽  
Chul Min Cho ◽  
Nicole Leclerc ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Neurofibrillary Tangles ◽  
Protein Tau ◽  
Microtubule Associated Protein Tau

Neuronal plasticity in hibernation and the proposed role of the microtubule-associated protein tau as a “master switch” regulating synaptic gain in neuronal networks

2013 ◽  
Vol 305 (5) ◽  
pp. R478-R489 ◽  
Author(s):  
Thomas Arendt ◽  
Torsten Bullmann
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Neuronal Networks ◽  
Mammalian Species ◽  
Synaptic Membrane ◽  
Reversible Phosphorylation ◽  
Learning Abilities ◽  
Protein Tau ◽  
Microtubule Associated Protein Tau ◽  
Synaptic Gain

The present paper provides an overview of adaptive changes in brain structure and learning abilities during hibernation as a behavioral strategy used by several mammalian species to minimize energy expenditure under current or anticipated inhospitable environmental conditions. One cellular mechanism that contributes to the regulated suppression of metabolism and thermogenesis during hibernation is reversible phosphorylation of enzymes and proteins, which limits rates of flux through metabolic pathways. Reversible phosphorylation during hibernation also affects synaptic membrane proteins, a process known to be involved in synaptic plasticity. This mechanism of reversible protein phosphorylation also affects the microtubule-associated protein tau, thereby generating a condition that in the adult human brain is associated with aggregation of tau protein to paired helical filaments (PHFs), as observed in Alzheimer's disease. Here, we put forward the concept that phosphorylation of tau is a neuroprotective mechanism to escape NMDA-mediated hyperexcitability of neurons that would otherwise occur during slow gradual cooling of the brain. Phosphorylation of tau and its subsequent targeting to subsynaptic sites might, thus, work as a kind of “master switch,” regulating NMDA receptor-mediated synaptic gain in a wide array of neuronal networks, thereby enabling entry into torpor. If this condition lasts too long, however, it may eventually turn into a pathological trigger, driving a cascade of events leading to neurodegeneration, as in Alzheimer's disease or other “tauopathies”.

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