ArticleThe Biochemical journal1997
Phosphorylation of tau by glycogen synthase kinase 3beta affects the ability of tau to promote microtubule self-assembly.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
28 citing papers in PubMed, 85 citations in OpenAlex.
- Fructose and insulin: A sweet sabotage hypothesis?Endocrine · 2025Review
- Cytomegalovirus infection induces Alzheimer's disease-associated alterations in tau.Journal of neurovirology · 2023Article
- Understanding Acquired Brain Injury: A Review.Biomedicines · 2022Review
- Aging and high-fat diet feeding lead to peripheral insulin resistance and sex-dependent changes in brain of mouse model of tau pathology THY-Tau22.Journal of neuroinflammation · 2021Article
- Alzheimer's Disease and Protein Kinases.Advances in experimental medicine and biology · 2021Article
- Glucose Regulates Microtubule Disassembly and the Dose of Insulin Secretion via Tau Phosphorylation.Diabetes · 2020Article
- Aberrant expression of the microtubule-associated protein tau is an independent prognostic feature in prostate cancer.BMC cancer · 2019Article
- Brain-Defective Insulin Signaling Is Associated to Late Cognitive Impairment in Post-Septic Mice.Molecular neurobiology · 2018Article
- Amyloid β-Exposed Human Astrocytes Overproduce Phospho-Tau and Overrelease It within Exosomes, Effects Suppressed by Calcilytic NPS 2143-Further Implications for Alzheimer's Therapy.Frontiers in neuroscience · 2017Article
- The rise and fall of insulin signaling in Alzheimer's disease.Metabolic brain disease · 2016Review
- Tau-induced neurodegeneration: mechanisms and targets.Neuroscience bulletin · 2014Review
- Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal models.Current pharmaceutical design · 2014Review
- Tau phosphorylation affects its axonal transport and degradation.Neurobiology of aging · 2013Article
- Link between cancer and Alzheimer disease via oxidative stress induced by nitric oxide-dependent mitochondrial DNA overproliferation and deletion.Oxidative medicine and cellular longevity · 2013Review
- WW domain-containing oxidoreductase promotes neuronal differentiation via negative regulation of glycogen synthase kinase 3β.Cell death and differentiation · 2012Article
- Tau as a therapeutic target for Alzheimer's disease.Current Alzheimer research · 2011Review
- Yeast as a model system to study tau biology.International journal of Alzheimer's disease · 2011Article
- Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.PloS one · 2011Article
- Article
- Functional implications of glycogen synthase kinase-3-mediated tau phosphorylation.International journal of Alzheimer's disease · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
To study the effects of phosphorylation by glycogen synthase kinase-3beta (GSK-3beta) on the ability of the microtubule-associated protein tau to promote microtubule self-assembly, tau isoform 1 (foetal tau) and three mutant forms of this tau isoform were investigated. The three mutant forms of tau had the following serine residues, known to be phosphorylated by GSK-3, replaced with alanine residues so as to preclude their phosphorylation: (1) Ser-199 and Ser-202 (Ser-199/202-->Ala), (2) Ser-235 (Ser-235-->Ala) and (3) Ser-396 and Ser-404 (Ser-396/404-->Ala). Wild-type tau and the mutant forms of tau were phosphorylated with GSK-3beta, and their ability to promote microtubule self-assembly was compared with the corresponding non-phosphorylated tau species. In the non-phosphorylated form, wild-type tau and all of the mutants affected the mean microtubule length and number concentrations of assembled microtubules in a manner consistant with enhanced microtubule nucleation. Phosphorylation of these tau species with GSK-3beta consistently reduced the ability of a given tau species to promote microtubule self-assembly, although the affinity of the tau for the microtubules was not greatly affected by phosphorylation since the tau species remained largely associated with the microtubules. This suggests that the regulation of microtubule assembly can be controlled by phosphorylation of tau at sites accessible to GSK-3beta by a mechanism that does not necessarily involve the dissociation of tau from the microtubules.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.