MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments
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MAP2 and tau exhibit microtubule-stabilizing activities that are implicated in the development and maintenance of neuronal axons and dendrites. The proteins share a homologous COOH-terminal domain, composed of three or four microtubule binding repeats separated by inter-repeats (IRs). To investigate how MAP2 and tau stabilize microtubules, we calculated 3D maps of microtubules fully decorated with MAP2c or tau using cryo-EM and helical image analysis. Comparing these maps with an undecorated microtubule map revealed additional densities along protofilament ridges on the microtubule exterior, indicating that MAP2c and tau form an ordered structure when they bind microtubules. Localization of undecagold attached to the second IR of MAP2c showed that IRs also lie along the ridges, not between protofilaments. The densities attributable to the microtubule-associated proteins lie in close proximity to helices 11 and 12 and the COOH terminus of tubulin. Our data further suggest that the evolutionarily maintained differences observed in the repeat domain may be important for the specific targeting of different repeats to either α or β tubulin. These results provide strong evidence suggesting that MAP2c and tau stabilize microtubules by binding along individual protofilaments, possibly by bridging the tubulin interfaces.
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Tau is a microtubule-associated protein that stabilizes microtubules by interacting with tubulin heterodimers, supporting axonal structure and neuronal morphology.
“The microtubule-associated protein tau (MAPT) was first identified as a key regulator of microtubule stability and assembly [1]. Tau stabilizes microtubules by interacting with tubulin heterodimers, thereby supporting axonal structure and maintaining neuronal morphology [2–4].”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [3]
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- Authors
- Al-Bassam, J., Ozer, R. S., Safer, D., Halpain, S., & Milligan, R. A.
- Affiliations
- 1Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037
- Scripps Research Institute (US)
- University of Pennsylvania (US)
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2002-06-24
- Volume
- 157
- Issue
- 7
- Pages
- 1187-1196
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2173547
- OpenAlex
- W2137036197
- Cited by
- 327
- References
- 69
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 12 · 2023: 10 · 2022: 9 · 2021: 20 · 2020: 12 · 2019: 18 · 2018: 21 · 2017: 15 · 2016: 15 · 2015: 11 · 2014: 19 · 2013: 17 · 2012: 17
- FWCI
- 5.35
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG05131, P50AG005131)
- National Institute of Mental Health (R29MH050861, F31MH012504, MH-50861, R01MH050861, MH-12504)
- National Institute of General Medical Sciences (GM 52468, R37GM052468, R01GM052468)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- MAP2, tau protein, microtubule stabilization, microtubule protofilaments, microtubule-binding repeats, MAP2c, microtubule-associated proteins, axon and dendrite development
- MeSH terms
- Animals, Binding Sites, Cattle, Cytoskeleton, Humans, Microtubule-Associated Proteins, Microtubules, Models, Biological, Models, Molecular, Mutation, Protein Binding, Recombinant Fusion Proteins, Tubulin, Sequence Alignment, tau Proteins, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Imaging, Three-Dimensional, Mice, Rats
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