Cited by 58Alzheimer's disease research and treatmentsMicrotubule and mitosis dynamicsNeuroinflammation and Neurodegeneration Mechanisms

Microtubule-Stimulated Phosphorylation of tau at Ser202 and Thr205 by cdk5 Decreases Its Microtubule Nucleation Activity

Wada, Y., Ishiguro, K., Itoh, T. J., Uchida, T., Hotani, H., Saito, T., Kishimoto, T., Hisanaga, S.-i.·1998·Journal of Biochemistry

Abstract

Phosphorylation of tau, a heat-stable neuron-specific microtubule-associated protein, by cdk5 was stimulated in the presence of microtubules (MTs). This stimulation was due to an increased phosphorylation rate and there was no increase in total amount of phosphorylation. Two-dimensional phosphopeptide map analysis showed that MTs stimulated phosphorylation of a specific peptide. Using Western blotting with antibodies that the recognized phosphorylation-dependent epitopes within tau, the phosphorylation sites stimulated by the presence of MTs were found to be Ser202 and Thr205 (numbered according to the human tau isoform containing 441 residues). MT-dependent phosphorylation at Thr205 was observed in situ in rat cerebrum primary cultured neurons. Stimulated phosphorylation at Ser202 and Thr205 decreased the MT-nucleation activity of tau, which is in contrast to MT-independent phosphorylation at Ser235 and Ser404.

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Crossref · 10.1093/oxfordjournals.jbchem.a022174

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Authors
Wada, Y., Ishiguro, K., Itoh, T. J., Uchida, T., Hotani, H., Saito, T., Kishimoto, T., & Hisanaga, S.-I.
Affiliations
Tokyo Institute of Technology (JP)
Venue
Journal of Biochemistry
Published
1998-10-01
Volume
124
Issue
4
Pages
738-746
ISSN
0021-924X (ISSN-L)
OpenAlex
W2040383902
Cited by
58
References
49
Citations by year
2026: 2 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 5 · 2019: 1 · 2018: 2 · 2017: 3 · 2016: 2 · 2014: 2 · 2013: 2 · 2012: 7
FWCI
0.82
Type
journal article
Language
en
Open access
closed
Locations
  • The Journal of Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords
tau protein, cyclin-dependent kinase 5, microtubule nucleation, microtubule-associated proteins, tau phosphorylation sites, phosphopeptide mapping
MeSH terms
Animals, Epitopes, Brain, Cells, Cultured, Embryo, Mammalian, Humans, Kinetics, Microtubules, Neurons, Peptide Mapping, Phosphopeptides, Phosphorylation, Serine, Swine, Threonine, Blotting, Western, Nocodazole, tau Proteins, Protein Serine-Threonine Kinases, Cyclin-Dependent Kinases, Cyclin-Dependent Kinase 5, Rats

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