The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding
Open accessAbstract
The interaction of actin with a synthetic peptide which corresponds to one of the repeated tubulin-binding sites present in tau and MAP-2 (microtubule-associated protein 2) proteins has been analysed. The analysis, which uses affinity chromatography of G-actin on a column containing the synthetic peptide, and the co-sedimentation and co-localization of F-actin and the peptide (as determined by immunoelectron microscopy), indicates that the part of the amino acid sequence of tau involved in the binding of tubulin is also involved in actin binding.
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More than one microtubule-binding repeat is believed to be required for bundling of filamentous actin.
“Because a single repeat interacts with both monomeric and filamentous actin, but does not bundle actin filaments, more than one microtubule-binding repeat is believed to be required for bundling of filamentous actin (F-actin)17.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [17]
The Results (page not provided) show that a peptide containing one tubulin-binding repeat binds G-actin and F-actin but does not bundle filaments. The authors suggest that bundling may require more than one actin-binding site; they do not establish that those sites must be multiple microtubule-binding repeats. (LLM, conf=0.85)
Experimental — accuracy not yet measuredA C-terminal fragment and a peptide corresponding to the second microtubule-binding repeat bind actin but are incapable of mediating actin cross-linking.
“For example, a C-terminal fragment and a peptide corresponding to the second microtubule-binding repeat bind actin, but are incapable of mediating actin cross-linking5, 17.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [17]
The Results report that the synthetic tau peptide binds G-actin and F-actin but does not bundle actin filaments. The Introduction and Discussion describe it as corresponding to one tubulin-binding repeat, without identifying it as the second. They report that a 32 kDa MAP-2 fragment binds actin, but do not establish that this C-terminal fragment cannot cross-link actin. (LLM, conf=0.86)
Experimental — accuracy not yet measuredA single microtubule-binding repeat interacts with both monomeric and filamentous actin but does not bundle actin filaments.
“Because a single repeat interacts with both monomeric and filamentous actin, but does not bundle actin filaments, more than one microtubule-binding repeat is believed to be required for bundling of filamentous actin (F-actin)17.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [17]
Binding to F-actin can be retained while cross-linking activity is disrupted.
“At the same time, binding to F-actin can be retained, but the cross-linking activity disrupted.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [17]
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Cites
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Canu, N., Dus, L., Barbato, C., Ciotti, M. T., Brancolini, C., Rinaldi, A. M., Novak, M., Cattaneo, A., Bradbury, A., & Calissano, P. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-18-07061.1998 · Cited by 232 · see citing works
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Tau co-organizes dynamic microtubule and actin networks
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Self-citation
- Authors
- Correas, I., Padilla, R., & Avila, J.
- Affiliations
- Consejo Superior de Investigaciones Científicas (ES)
- Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain.
- ORCID
- Correas, I
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1990-07-01
- Volume
- 269
- Issue
- 1
- Pages
- 61-64
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1131531
- OpenAlex
- W2236551278
- Cited by
- 144
- References
- 1
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 1 · 2022: 4 · 2021: 1 · 2020: 6 · 2019: 12 · 2018: 3 · 2017: 8 · 2016: 6 · 2015: 7 · 2014: 3 · 2013: 1 · 2012: 3
- FWCI
- 4.84
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (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 › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- tau protein, MAP2, microtubule-associated proteins, tubulin binding site, actin binding, synthetic peptides
- MeSH terms
- Actins, Animals, Binding Sites, Cattle, Chromatography, Affinity, Immunohistochemistry, Microscopy, Electron, Microtubule-Associated Proteins, Polymers, Tubulin, tau Proteins
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