The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases.
Reads0
Chats0
TLDR
PP2A and PP2B (or closely related phosphatases) may regulate the phosphorylation state of adult tau isoforms in vivo, and the generation of PHF-tau in the AD brain may result from the abnormal inactivation of similar phosphatasing.About:
This article is published in Journal of Biological Chemistry.The article was published on 1994-12-09 and is currently open access. It has received 142 citations till now. The article focuses on the topics: Okadaic acid & Phosphorylation.read more
Citations
More filters
Journal ArticleDOI
Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
TL;DR: Tau proteins are the major constituents of intraneuronal and glial fibrillar lesions described in Alzheimer's disease and numerous neurodegenerative disorders referred as 'tauopathies' as discussed by the authors.
Journal ArticleDOI
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yasumasa Yoshiyama,Makoto Higuchi,Bin Zhang,Shu-Ming Huang,Nobuhisa Iwata,Takaomi C. Saido,Jun Maeda,Tetsuya Suhara,John Q. Trojanowski,Virginia M.-Y. Lee +9 more
TL;DR: In this paper, the authors studied wild-type and P301S mutant human tau transgenic (Tg) mice and found that tangle formation was preceded by microglial activation.
Journal ArticleDOI
Lithium Reduces Tau Phosphorylation by Inhibition of Glycogen Synthase Kinase-3
TL;DR: Using cultured human NT2N neurons, it is demonstrated that lithium reduces the phosphorylation of t Tau, enhances the binding of tau to microtubules, and promotes microtubule assembly through direct and reversible inhibition of glycogen synthase kinase-3.
Journal ArticleDOI
Regulated phosphorylation and dephosphorylation of tau protein : effects on microtubule interaction, intracellular trafficking and neurodegeneration
TL;DR: What is known about tau phosphorylation in the context of both normal cellular function and dysfunction is summarized to help determine what is causal and what is coincidental in Alzheimer's disease, and may lead to identification of therapeutic targets for halting the progression of paired helical filament formation.
Journal ArticleDOI
Phosphorylation of Microtubule-associated Protein Tau Is Regulated by Protein Phosphatase 2A in Mammalian Brain IMPLICATIONS FOR NEUROFIBRILLARY DEGENERATION IN ALZHEIMER'S DISEASE
TL;DR: It is suggested that protein phosphatase 2A participates in regulation of tau phosphorylation, processing, and function in vivo and can lead to Alzheimer-like abnormal hyperphosphorylated tau.
References
More filters
PatentDOI
Measurement of protein using bicinchoninic acid
TL;DR: This new method maintains the high sensitivity and low protein-to-protein variation associated with the Lowry technique and demonstrates a greater tolerance of the bicinchoninate reagent toward such commonly encountered interferences as nonionic detergents and simple buffer salts.
Journal ArticleDOI
Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology
Inge Grundke-Iqbal,Khalid Iqbal,Yunn-Chyn Tung,Maureen Quinlan,Henryk M. Wisniewski,Lester I. Binder +5 more
TL;DR: It is suggested that tau in Alzheimer brain is an abnormally phosphorylated protein component of PHF, the two major locations of paired-helical filaments in Alzheimer disease brain.
Journal ArticleDOI
A protein factor essential for microtubule assembly
TL;DR: The unique ability of tau to restore the normal features of in vitro microtubules assembly makes it likely that tau is a major regulator of microtubule formation in cells.
Journal ArticleDOI
The structure and regulation of protein phosphatases
TL;DR: Four major serine/threonine-specific protein phosphatase catalytic subunits are present in the cytoplasm of animal cells and have broad and overlapping specificities in vitro, and account for virtually all measurable activity in tissue extracts toward a variety of phosphoproteins that regulate metabolism, muscle contractility, and other processes.
Journal ArticleDOI
Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
TL;DR: Antisera raised against synthetic peptides corresponding to these different human tau isoforms demonstrate that multiple tau protein isoforms are incorporated into the neurofibrillary tangles of Alzheimer's disease.