Microtubule Acetylation Is Required for Mechanosensation in Drosophila [PDF]
Cell Reports, 2018 Summary: At the cellular level, α-tubulin acetylation alters the structure of microtubules to render them mechanically resistant to compressive forces. How this biochemical property of microtubule acetylation relates to mechanosensation remains unknown ...
Yun Peng, Jay Parrish, Richard Superfine
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Microtubule acetylation dyshomeostasis in Parkinson’s disease [PDF]
Translational Neurodegeneration, 2023 The inter-neuronal communication occurring in extensively branched neuronal cells is achieved primarily through the microtubule (MT)-mediated axonal transport system.
Padmashri Naren +6 more
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Microtubule damage shapes the acetylation gradient
Nature CommunicationsThe properties of single microtubules within the microtubule network can be modulated through post-translational modifications (PTMs), including acetylation within the lumen of microtubules.
Charlotte Aumeier, Marie-Claire Velluz
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The Ability to Induce Microtubule Acetylation Is a General Feature of Formin Proteins [PDF]
PLoS ONE, 2012 Cytoplasmic microtubules exist as distinct dynamic and stable populations within the cell. Stable microtubules direct and maintain cell polarity and it is thought that their stabilization is dependent on coordinative organization between the microtubule ...
Jonathan M Lee +2 more
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p27 controls autophagic vesicle trafficking in glucose-deprived cells via the regulation of ATAT1-mediated microtubule acetylation [PDF]
Cell Death and Disease, 2021 The cyclin-dependent kinase inhibitor p27Kip1 (p27) has been involved in promoting autophagy and survival in conditions of metabolic stress. While the signaling cascade upstream of p27 leading to its cytoplasmic localization and autophagy induction has ...
Ada Nowosad +7 more
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Drosophila CG17003/leaky (lky) is required for microtubule acetylation in early germ cells in Drosophila ovary. [PDF]
PLoS ONE, 2022 Microtubule acetylation is found in populations of stable, long-lived microtubules, occurring on the conserved lysine 40 (K40) residue of α-tubulin by α-tubulin acetyltransferases (αTATs).
Matthew Antel +3 more
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Microtubule acetylation is not required for HIV-1 infection or TRIM69-mediated restriction of HIV-1 infection [PDF]
Journal of VirologyMicrotubule acetylation, a post-translational modification catalyzing the addition of acetyl groups to lysine residues on alpha tubulin, confers mechanical resilience to microtubules and influences intracellular cargo transport.
Drew M. Lichon +3 more
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Luminal Localization of α-tubulin K40 Acetylation by Cryo-EM Analysis of Fab-Labeled Microtubules [PDF]
PLoS ONE, 2012 The αβ-tubulin subunits of microtubules can undergo a variety of evolutionarily-conserved post-translational modifications (PTMs) that provide functional specialization to subsets of cellular microtubules. Acetylation of α-tubulin residue Lysine-40 (K40)
Kristen J Verhey +2 more
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Suppression of microtubule acetylation mediates the anti-leukemic effect of CDK9 inhibition [PDF]
Cancer Cell InternationalCyclin-dependent kinase 9 (CDK9) is a crucial component of transcription and potential target for anti-cancer therapies, particularly for hematological malignancies.
Xi Xie +17 more
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Microtubule lattice conformation and integrity regulate α-tubulin acetylation [PDF]
Communications BiologyMicrotubule acetylation of lysine 40 of α-tubulin is a hallmark of stable microtubules. This luminal modification is catalyzed by α-tubulin acetyltransferase 1 (αTAT1) and reversed by histone deacetylase 6 (HDAC6).
Cornelia Egoldt +3 more
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