Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure [PDF]
Molecular Biology of the Cell, 2014 Tubulin undergoes posttranslational modifications proposed to specify microtubule subpopulations for particular functions. Most of these modifications occur on the C-termini of tubulin and may directly affect the binding of microtubule-associated proteins (MAPs) or motors.
Howes, Stuart C +4 more
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Conserved Lysine Acetylation within the Microtubule-Binding Domain Regulates MAP2/Tau Family Members. [PDF]
PLoS ONE, 2016 Lysine acetylation has emerged as a dominant post-translational modification (PTM) regulating tau proteins in Alzheimer's disease (AD) and related tauopathies.
Andrew W Hwang +6 more
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S6K1 Is Indispensible for Stress-Induced Microtubule Acetylation and Autophagic Flux. [PDF]
Cells, 2021 Autophagy is a specific macromolecule and organelle degradation process. The target macromolecule or organelle is first enclosed in an autophagosome, and then delivered along acetylated microtubules to the lysosome. Autophagy is triggered by stress and largely contributes to cell survival.
Hać A +2 more
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Non-catalytic allostery in α-TAT1 by a phospho-switch drives dynamic microtubule acetylation. [PDF]
J Cell Biol, 2022 International audienceSpatiotemporally 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 ...
Deb Roy A +5 more
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Marginal band microtubules are acetylated by αTAT1 [PDF]
Platelets, 2020 The discoid shape of resting platelets is maintained by a peripheral, circular bundle of microtubules called marginal band. Marginal band microtubules are acetylated on lysine 40 of the alpha-tubulin subunits. We have previously shown that the deacetylase HDAC6 is responsible for tubulin deacetylation in platelets and that the hyperacetylated state of ...
Ribba, Anne-Sophie +9 more
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Microtubule acetylation and PERK activation facilitate eribulin-induced mitochondrial calcium accumulation and cell death [PDF]
Cellular and Molecular Life SciencesPanseon Ko +2 more
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A Slow Dance for Microtubule Acetylation [PDF]
Cell, 2014 Microtubules contribute to diverse cellular processes through balancing dynamic, short-lived and stable, long-lived populations. One way in which long-lived microtubules are marked is by posttranslational acetylation of α-tubulin by tubulin acetyltransferase (TAT). Szyk et al.
Kull, F. Jon, Sloboda, Roger D.
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DYRK1B regulates Hedgehog-induced microtubule acetylation. [PDF]
Cell Mol Life Sci, 2019 The posttranslational modification (PTM) of tubulin subunits is important for the physiological functions of the microtubule (MT) cytoskeleton. Although major advances have been made in the identification of enzymes carrying out MT-PTMs, little knowledge is available on how intercellular signaling molecules and their associated pathways regulate MT-PTM-
Singh R +10 more
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Coordination of microtubule acetylation and the actin cytoskeleton by formins. [PDF]
Cell Mol Life Sci, 2018 The acetylation of the lysine 40 residue of α-tubulin was described more than 30 years ago and has been the subject of intense research ever since. Although the exact function of this covalent modification of tubulin in the cell remains unknown, it has been established that tubulin acetylation confers resilience to mechanical stress on the microtubules.
Fernández-Barrera J, Alonso MA.
europepmc +3 more sources
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)
Virupakshi Soppina +3 more
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