The microtubule-associated protein tau is strongly linked to Alzheimer’s disease, but the physiological functions of tau on microtubules remain unclear. New experiments reveal that tau recognizes and alters the conformation of the underlying microtubule lattice by forming envelopes that surround its surface, suggestive of a novel role for tau in cell physiology.
This is a preview of subscription content, access via your institution
Access options
Access Nature and 54 other Nature Portfolio journals
Get Nature+, our best-value online-access subscription
$29.99 / 30 days
cancel any time
Subscribe to this journal
Receive 12 print issues and online access
$259.00 per year
only $21.58 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Hernandez, F. et al. Tau aggregation. Neuroscience https://doi.org/10.1016/j.neuroscience.2022.04.024 (2022). This review presents background information on tau aggregation in human disease.
Siahaan, V. et al. Kinetically distinct phases of tau on microtubules regulate kinesin motors and severing enzymes. Nat. Cell Biol. 21, 1086–1092 (2019). This paper, along with ref. 3, reports the novel activity of tau envelope formation on microtubules.
Tan, R. et al. Microtubules gate tau condensation to spatially regulate microtubule functions. Nat. Cell Biol. 21, 1078–1085 (2019). This paper, along with ref. 2, reports the novel activity of tau envelope formation on microtubules.
de Jager, L., Jansen, K.I., Kapitein, L.C., Förster, F. & Howes, S.C. Increased microtubule lattice spacing correlates with selective binding of kinesin-1 in cells. Preprint at bioRxiv https://doi.org/10.1101/2022.05.25.493428 (2022). This recent preprint reveals variations in microtubule lattice spacing within living cells.
Chaaban, S. et al. The structure and dynamics of C. elegans tubulin reveals the mechanistic basis of microtubule growth. Dev. Cell 47, 191–204.e8 (2018). This paper reports that the GDP microtubule lattice is expanded in Caenorhabditis elegans microtubules.
Additional information
Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
This is a summary of: Siahaan, V. et al. Microtubule lattice spacing governs cohesive envelope formation of tau family proteins. Nat. Chem. Biol. https://doi.org/10.1038/s41589-022-01096-2 (2022).
Rights and permissions
About this article
Cite this article
Alzheimer’s disease–implicated protein tau puts the squeeze on microtubules. Nat Chem Biol 18, 1172–1173 (2022). https://doi.org/10.1038/s41589-022-01097-1
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41589-022-01097-1
