ArticleThe Journal of cell biology2022
Non-catalytic allostery in α-TAT1 by a phospho-switch drives dynamic microtubule acetylation.
Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- OptoTAT reveals microtubule acetylation as a rapid trigger for GEF-H1-mediated cell migration.The Journal of cell biology · 2026Article
- A genetically encoded microtubule bundler for causal dissection of microtubule bundling in cells.bioRxiv : the preprint server for biology · 2026Article
- Metabolic STAMP for deciphering GPCR-regulated insulin secretion by pancreatic β cells.bioRxiv : the preprint server for biology · 2025Article
- Tubulin acetyltransferases access and modify the microtubule luminal K40 residue through anchors in taxane-binding pockets.Nature structural & molecular biology · 2025Article
- Optogenetically Induced Microtubule Acetylation Unveils the Molecular Dynamics of Actin-Microtubule Crosstalk in Directed Cell Migration.bioRxiv : the preprint server for biology · 2024Article
- Microtubule-associated protein MAP7 promotes tubulin posttranslational modifications and cargo transport to enable osmotic adaptation.Developmental cell · 2024Article
- The α-tubulin acetyltransferase ATAT1: structure, cellular functions, and its emerging role in human diseases.Cellular and molecular life sciences : CMLS · 2024Review
- Non-catalytic role of phosphoinositide 3-kinase in mesenchymal cell migration through non-canonical induction of p85β/AP2-mediated endocytosis.Nature communications · 2024Article
- Macromolecular Crowding Tailors the Microtubule Cytoskeleton Through Tubulin Modifications and Microtubule-Associated Proteins.bioRxiv : the preprint server for biology · 2023Article
- Review
- Regulation of cellular contractile force, shape and migration of fibroblasts by oncogenes and Histone deacetylase 6.Frontiers in molecular biosciences · 2023Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Spatiotemporally dynamic microtubule acetylation underlies diverse physiological and pathological events. Despite its ubiquity, the molecular mechanisms that regulate the sole microtubule acetylating agent, α-tubulin-N-acetyltransferase-1 (α-TAT1), remain obscure. Here, we report that dynamic intracellular localization of α-TAT1 along with its catalytic activity determines efficiency of microtubule acetylation. Specifically, we newly identified a conserved signal motif in the intrinsically disordered C-terminus of α-TAT1, consisting of three competing regulatory elements-nuclear export, nuclear import, and cytosolic retention. Their balance is tuned via phosphorylation by CDK1, PKA, and CK2, and dephosphorylation by PP2A. While the unphosphorylated form binds to importins and resides both in cytosol and nucleus, the phosphorylated form binds to specific 14-3-3 adapters and accumulates in the cytosol for maximal substrate access. Unlike other molecules with a similar phospho-regulated signal motif, α-TAT1 uniquely uses the nucleus as a hideout. This allosteric spatial regulation of α-TAT1 function may help uncover a spatiotemporal code of microtubule acetylation in normal and aberrant cell behavior.
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Registered trials
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