Cited by 501Alzheimer's disease research and treatmentsMicrotubule and mitosis dynamicsNeuroinflammation and Neurodegeneration Mechanisms

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The microtubule binding domain of tau protein

Lee, Gloria, Neve, Rachael L., Kosik, Kenneth S.·1989·Neuron

DOI 10.1016/0896-6273(89)90050-0

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Abstract

Tau protein is a microtubule-associated protein implicated in the spatial and temporal specification of microtubules and has been found in the neurofibrillary tangles of Alzheimer's disease. Determination of tau protein structure has revealed three 18 amino acid repeated sequences hypothesized to be tubulin binding sites. Using tau cDNA clones from human fetal brain, we employed E. coli expression systems to synthesize tau protein and fragments of tau protein in order to identify the microtubule binding site. A fragment containing the three repeated sequences binds microtubules, while the amino-terminal half of the protein does not bind. Fragments containing two or one repeat are also capable of binding, indicating that the basic tubulin interacting unit is one repeat.

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Khodja, L. A. (2022) · theses.fr (ABES) · doi:10.70675/d8b90a94z5fbdz4ca2za1edz18751d5575da
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Furhang, R., Morrone, R., Nikulina, E., Jere, M., Kaur, A., Nayab, F., Saito, T., Saido, T. C., & Bergold, P. J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.08.737276
RNA Splicing Dysregulation in Parkinson’s Disease
Bruno, M. G., Menichetti, G., Valentino, A., Javaid, A., Belpinati, F., Ruggiero, A., Valenti, M. T., Paolone, G., Cavaliere, F., Trabetti, E., et al. (2026) · Genes · doi:10.3390/genes17080911
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Molecular Mechanisms of Frontotemporal Lobar Degeneration
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Functional Study of the Threonine Phosphorylation and the Transcriptional Coactivator Role of P68 RNA Helicase
Dey, H. T. (2012) · Digital Archive @ GSU · doi:10.57709/3489823

Authors: Lee, G., Neve, R. L., & Kosik, K. S.
Affiliations: Brigham and Women's Hospital (US)
Boston Children's Hospital (US)
ORCID: Lee, Gloria
Neve, Rachael L.
Kosik, Kenneth S.
Venue: Neuron
Publisher: Elsevier BV
Published: 1989-06
Volume: 2
Issue: 6
Pages: 1615-1624
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/0896-6273(89)90050-0
OpenAlex: W1972355725
Cited by: 500
References: 66
Citations by year: 2026: 8 · 2025: 13 · 2024: 13 · 2023: 19 · 2022: 12 · 2021: 19 · 2020: 14 · 2019: 17 · 2018: 13 · 2017: 13 · 2016: 8 · 2015: 12 · 2014: 13 · 2013: 13 · 2012: 13
FWCI: 14.86
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r29gm039300-05, 5r01ag006601-13)
National Institute on Aging (R01 AG06601-01)
National Institute of General Medical Sciences (R29 GM39300-01)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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, microtubule-binding site, microtubule-associated proteins, tubulin binding, neurofibrillary tangles, Alzheimer's disease, protein structure
MeSH terms: Amino Acid Sequence, Base Sequence, Binding Sites, DNA, Humans, Microtubule-Associated Proteins, Microtubules, Molecular Sequence Data, Protein Binding, Recombinant Fusion Proteins, Repetitive Sequences, Nucleic Acid, Sequence Homology, Nucleic Acid, Tubulin, tau Proteins

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The microtubule binding domain of tau protein

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