ArticleJournal of protein chemistry1995
Tau protein kinase I/GSK-3 beta/kinase FA in heparin phosphorylates tau on Ser199, Thr231, Ser235, Ser262, Ser369, and Ser400 sites phosphorylated in Alzheimer disease brain.
Article in Journal of protein chemistry, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 53 citations in OpenAlex.
- Do tau-synaptic long-term depression interactions in the hippocampus play a pivotal role in the progression of Alzheimer's disease?Neural regeneration research · 2023Review
- Mitochondrial Kinases and the Role of Mitochondrial Protein Phosphorylation in Health and Disease.Life (Basel, Switzerland) · 2021Review
- Sulfhydration of AKT triggers Tau-phosphorylation by activating glycogen synthase kinase 3β in Alzheimer's disease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Reduction of PINK1 or DJ-1 impair mitochondrial motility in neurites and alter ER-mitochondria contacts.Journal of cellular and molecular medicine · 2018Article
- Protein tau: prime cause of synaptic and neuronal degeneration in Alzheimer's disease.International journal of Alzheimer's disease · 2012Article
- Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms.Biochemistry · 2011Article
- Tau potentiates nerve growth factor-induced mitogen-activated protein kinase signaling and neurite initiation without a requirement for microtubule binding.The Journal of biological chemistry · 2010Article
- High-content siRNA screening of the kinome identifies kinases involved in Alzheimer's disease-related tau hyperphosphorylation.BMC genomics · 2010Article
- Pseudohyperphosphorylation causing AD-like changes in tau has significant effects on its polymerization.Biochemistry · 2009Article
- Pre-assembled tau filaments phosphorylated by GSK-3b form large tangle-like structures.Neurobiology of disease · 2008Article
- Tau phosphorylation by GSK-3beta promotes tangle-like filament morphology.Molecular neurodegeneration · 2007Article
- Regulation of phosphorylation of tau by cyclin-dependent kinase 5 and glycogen synthase kinase-3 at substrate level.FEBS letters · 2006Article
- Discovery of compounds that will prevent tau pathology.Journal of molecular neuroscience : MN · 2002Review
- Levels of nonphosphorylated and phosphorylated tau in cerebrospinal fluid of Alzheimer's disease patients : an ultrasensitive bienzyme-substrate-recycle enzyme-linked immunosorbent assay.The American journal of pathology · 2002Article
- Phosphorylated tau can promote tubulin assembly.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease.Molecular biology of the cell · 1998Article
- Phosphorylation of tau by glycogen synthase kinase 3beta affects the ability of tau to promote microtubule self-assembly.The Biochemical journal · 1997Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previously, tau protein kinase I/glycogen synthase kinase-3 beta/kinase FA(TPKI/GSK-3 beta/FA) was identified as a brain microtubule-associated tau kinase possibly involved in the Alzheimer disease-like phosphorylation of tau. In this report, we find that the TPKI/GSK-3 beta/FA can be stimulated to phosphorylate brain tau up to 8.5 mol of phosphates per mol of protein by heparin, a polyanion compound. Tryptic digestion of 32P-labeled tau followed by high-performance liquid chromatography and high-voltage electrophoresis/thin-layer chromatography reveals 12 phosphopeptides. Phosphoamino acid analysis together with sequential manual Edman degradation and peptide sequence analysis further reveals that TPKI/GSK-3 beta/FA after heparin potentiation phosphorylates tau on sites of Ser199, Thr231, Ser235, Ser262, Ser396, and Ser400, which are potential sites abnormally phosphorylated in Alzheimer tau and potent sites responsible for reducing microtubule binding possibly involved in neuronal degeneration. The results provide initial evidence that TPKI/GSK-3 beta/FA after heparin potentiation may represent one of the most potent systems possibly involved in the abnormal phosphorylation of PHF-tau and neuronal degeneration in Alzheimer disease brains.
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