ArticleNature communications2024
Microtubule damage shapes the acetylation gradient.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Post-Translational Modifications of Tubulin in Oocyte Maturation and Female Infertility.Cytoskeleton (Hoboken, N.J.) · 2026Review
- Microtubule lattice conformation and integrity regulate α-tubulin acetylation.Communications biology · 2026Article
- Rules of the road: how to turn off kinesin motors.The Biochemical journal · 2026Review
- Cell type transcriptomic modules reveal shared molecular mechanisms in Alzheimer's and Parkinson's disease.GigaScience · 2026Article
- Regulation of apoptosis, ferroptosis, and pyroptosis mediated by acetylation.Cell death discovery · 2026Review
- Targeting microglia microtubules: cytoskeletal remodeling as a druggable hub in neuroinflammation and neurodegeneration.Frontiers in neuroscience · 2026Review
- Microtubule architecture connects AMOT stability to YAP/TAZ mechanotransduction and Hippo signalling.Nature cell biology · 2025Article
- Optogenetic and chemical genetic tools for rapid repositioning of vimentin intermediate filaments.The Journal of cell biology · 2025Article
- How does the tubulin code facilitate directed cell migration?Biochemical Society transactions · 2025Review
- Emerging roles for tubulin PTMs in neuronal function and neurodegenerative disease.Current opinion in neurobiology · 2025Review
- The alpha tubulin acetyltransferasemicroPublication biology · 2025Article
- Tubulin Acetylation: A Critical Regulator of Microtubule Function.Results and problems in cell differentiation · 2025Review
- Microtubule shaft integrity emerges as a crucial determinant of the acetylation pattern.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Tubulin Acetylation and the Cellular Mechanosensing and Stress Response.Results and problems in cell differentiation · 2025Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The properties of single microtubules within the microtubule network can be modulated through post-translational modifications (PTMs), including acetylation within the lumen of microtubules. To access the lumen, the enzymes could enter through the microtubule ends and at damage sites along the microtubule shaft. Here we show that the acetylation profile depends on damage sites, which can be caused by the motor protein kinesin-1. Indeed, the entry of the deacetylase HDAC6 into the microtubule lumen can be modulated by kinesin-1-induced damage sites. In contrast, activity of the microtubule acetylase αTAT1 is independent of kinesin-1-caused shaft damage. On a cellular level, our results show that microtubule acetylation distributes in an exponential gradient. This gradient results from tight regulation of microtubule (de)acetylation and scales with the size of the cells. The control of shaft damage represents a mechanism to regulate PTMs inside the microtubule by giving access to the lumen.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.