Normal and Pathological Tau Proteins as Factors for Microtubule Assembly

doi:10.1016/S0074-7696(08)62588-7

International Review of Cytology

Volume 171, 1997, Pages 167-224

https://doi.org/10.1016/S0074-7696(08)62588-7 Get rights and content

Tau proteins are microtubule-associated proteins. They regulate the dynamics of the microtubule network, especially involved in the axonal transport and neuronal plasticity. Tau proteins belong to a family of developmentally regulated isoforms generated by alternative splicing and phosphorylation. This generates several Tau variants that interact with tubulin and other proteins. Therefore, Tau proteins are influenced by many physiological regulations. Tau proteins are also powerful markers of the neuronal physiological state. Their degree of phosphorylation is a good marker of cell integrity. It is heavily disturbed in numerous neurodegenerative disorders, leading to a collapse of the microtubule network and the presence of intraneuronal lesions resulting from Tau aggregation. However, different biochemical and immunological patterns of pathological Tau proteins found among neurodegenerative disorders are useful markers for the understanding of the role of Tau protein isoforms and the diagnosis of these pathological conditions.

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Normal and Pathological Tau Proteins as Factors for Microtubule Assembly

Acta Psychiatr. Scand.

J. Biol. Chem.

Mol. Brain Res.

FEBS Lett.

Int. J. Dev. Neurosci.

Exp. Neurol.

Neuron

Neurobiol. Aging

Neurosci. Lett.

Neuron

Neuron

Biochimie.

J. Biol. Chem.

Biomed. Pharmacother.

J. Neurol. Sci.

Brain Res.

J. Biol. Chem.

Neuroscience

Dev. Brain Res.

FEBS Lett.

Dev. Brain Res.

J. Neurol. Sci.

Brain Res.

Neuron

Neuron

Neurosci. Lett.

J. Biol. Chem.

Exp. Cell Res.

J. Biol. Chem.

Microtubule-associated proteins connect microtubules and neurofilaments in vitro

Biochemistry

Unusual argyrophilic glial cells in progressive supranuclear palsy

Neurodegeneration

Subcortical dementia

Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer's disease

Proc. Natl. Acad. Sci. USA

Structure and novel exons of the human-Tau gene

Biochemistry

Relative exon affinities and suboptimal splice site signals lead to non-equivalence of two cassette exon

Nucleic Acids Res.

A tau promoter region without neuronal specificity

J. Neurochem.

Tau is a glycoprotein

Soc. Neurosci. Abstr.

Twisted tubulofilaments of inclusion body myositis muscle resemble paired helical filaments of Alzheimer brain and contain hyperphosphorylated tau

Am. J. Pathol.

Paired helical filament Tau (PHFtau) in Niemann-Pick type C disease is similar to PHFTau in Alzheimer's disease

Acta Neuropathol

The distribution of Tau in the mammalian central nervous system

J. Cell Biol.

Microcebus murinus, a convenient laboratory animal model for the study of Alzheimer's disease

Alzheimer's Res.

Polyglutamylation of tubulin as a progressive regulator of in vitro interaction between the microtubule-associated protein Tau and tubulin

Biochemistry

Regional distribution of neurofibrillary tangles and senile plaques in the cerebral cortex of elderly patients—A quantitative evaluation of a one-year-autopsy population from a geriatric hospital

Cerebral Cortex

Distribution of Big Tau in the central nervous system of the adult and developing rat

J. Comp. Neurol.

Neuropil threads occur in dendrites of tangle-bearing nerve cells

Neuropathol. Appl. Neurol.

Occurrence of neuropils threads in the senile human brain and in Alzheimer's disease. A 3rd location of paired helical filaments outside of neurofibrillary tangles and neuritic plaques

Neurosci. Lett.

Presence of Tau in isolated nuclei from human brain

Neurobiol. Aging

Interaction of Tau with the neural plasma membrane mediated by tau's amino-terminal projection domain

J. Cell Biol.

Immunological detection of Tau protein in neurofibrillary tangles of Alzheimer's disease

Arch. Biol.

Recent findings in Pick's disease

Prog. Neuropathol.