ArticleCurrent biology : CB2012
Genetically separable functions of the MEC-17 tubulin acetyltransferase affect microtubule organization.
Article in Current biology : CB, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
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96 citing papers in PubMed, 160 citations in OpenAlex.
- Prognostic, diagnostic and therapeutic value of the cancer tubulin code.Cancer metastasis reviews · 2026Review
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- How does the tubulin code facilitate directed cell migration?Biochemical Society transactions · 2025Review
- Cryo-ET suggests tubulin chaperones form a subset of microtubule lumenal particles with a role in maintaining neuronal microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Tubulin Acetylation: A Critical Regulator of Microtubule Function.Results and problems in cell differentiation · 2025Review
- Computational and experimental identification of putative αTAT1 modulators: implications for nervous system function.Frontiers in pharmacology · 2025Article
- C. elegans touch receptor neurons direct mechanosensory complex organization via repurposing conserved basal lamina proteins.Current biology : CB · 2024Article
- Article
- The α-tubulin acetyltransferase ATAT1: structure, cellular functions, and its emerging role in human diseases.Cellular and molecular life sciences : CMLS · 2024Review
- Review
- Article
- Lumenal components of cytoplasmic microtubules.Biochemical Society transactions · 2022Review
- Synaptic branch stability is mediated by non-enzymatic functions of MEC-17/αTAT1 and ATAT-2.Scientific reports · 2022Article
- Acetylated α-tubulin K394 regulates microtubule stability to shape the growth of axon terminals.Current biology : CB · 2022Article
- The Expression and Function of Tubulin Isotypes inFrontiers in cell and developmental biology · 2022Review
- Review
- The tubulin code specializes neuronal cilia for extracellular vesicle release.Developmental neurobiology · 2021Review
- Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Article
- Dispensability of Tubulin Acetylation for 15-protofilament Microtubule Formation in the Mammalian Cochlea.Cell structure and function · 2021Article
36 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundMicrotubules (MTs) are formed from the lateral association of 11-16 protofilament chains of tubulin dimers, with most cells containing 13-protofilament (13-p) MTs. How these different MTs are formed is unknown, although the number of protofilaments may depend on the nature of the α- and β-tubulins.
resultsHere we show that the enzymatic activity of the Caenorhabiditis elegans α-tubulin acetyltransferase (α-TAT) MEC-17 allows the production of 15-p MTs in the touch receptor neurons (TRNs) MTs. Without MEC-17, MTs with between 11 and 15 protofilaments are seen. Loss of this enzymatic activity also changes the number and organization of the TRN MTs and affects TRN axonal morphology. In contrast, enzymatically inactive MEC-17 is sufficient for touch sensitivity and proper process outgrowth without correcting the MT defects. Thus, in addition to demonstrating that MEC-17 is required for MT structure and organization, our results suggest that the large number of 15-p MTs, normally found in the TRNs, is not essential for mechanosensation.
conclusionThese experiments reveal a specific role for α-TAT in the formation of MTs and in the production of higher order MTs arrays. In addition, our results indicate that the α-TAT protein has functions that require acetyltransferase activity (such as the determination of protofilament number) and others that do not (presence of internal MT structures).
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