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Journal articles on the topic 'Acetylation α-Tubulin'

Author: Grafiati

Published: 22 June 2024

Last updated: 31 July 2025

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1

Chu, Chih-Wen, Fajian Hou, Junmei Zhang та ін. "A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation". Molecular Biology of the Cell 22, № 4 (2011): 448–56. http://dx.doi.org/10.1091/mbc.e10-03-0203.

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Dynamic instability is a critical property of microtubules (MTs). By regulating the rate of tubulin polymerization and depolymerization, cells organize the MT cytoskeleton to accommodate their specific functions. Among many processes, posttranslational modifications of tubulin are implicated in regulating MT functions. Here we report a novel tubulin acetylation catalyzed by acetyltransferase San at lysine 252 (K252) of β-tubulin. This acetylation, which is also detected in vivo, is added to soluble tubulin heterodimers but not tubulins in MTs. The acetylation-mimicking K252A/Q mutants were inc

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2

Calogero, Alessandra Maria, Milo Jarno Basellini, Huseyin Berkcan Isilgan та ін. "Acetylated α-Tubulin and α-Synuclein: Physiological Interplay and Contribution to α-Synuclein Oligomerization". International Journal of Molecular Sciences 24, № 15 (2023): 12287. http://dx.doi.org/10.3390/ijms241512287.

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Emerging evidence supports that altered α-tubulin acetylation occurs in Parkinson’s disease (PD), a neurodegenerative disorder characterized by the deposition of α-synuclein fibrillary aggregates within Lewy bodies and nigrostriatal neuron degeneration. Nevertheless, studies addressing the interplay between α-tubulin acetylation and α-synuclein are lacking. Here, we investigated the relationship between α-synuclein and microtubules in primary midbrain murine neurons and the substantia nigra of post-mortem human brains. Taking advantage of immunofluorescence and Proximity Ligation Assay (PLA),

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Yang, Wulin, Xiangxiang Guo, Shermaine Thein та ін. "Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of α-tubulin". Biochemical Journal 449, № 3 (2013): 605–12. http://dx.doi.org/10.1042/bj20121121.

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Cytoskeleton remodelling is a prerequisite step for the morphological transition from preadipocytes to mature adipocytes. Although microtubules play a pivotal role in organizing cellular structure, regulation of microtubule dynamics during adipogenesis remains unclear. In the present paper we show that acetylation of α-tubulin is up-regulated during adipogenesis, and adipocyte development is dependent on α-tubulin acetylation, as expression of an acetylation-resistant α-tubulin mutant significantly inhibits adipogenesis. Moreover, acetylation of α-tubulin is under the control of the acetyltran

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4

Carmona, Bruno, H. Susana Marinho, Catarina Lopes Matos, Sofia Nolasco, and Helena Soares. "Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation." Biology 12, no. 4 (2023): 561. http://dx.doi.org/10.3390/biology12040561.

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Microtubules (MTs), dynamic polymers of α/β-tubulin heterodimers found in all eukaryotes, are involved in cytoplasm spatial organization, intracellular transport, cell polarity, migration and division, and in cilia biology. MTs functional diversity depends on the differential expression of distinct tubulin isotypes and is amplified by a vast number of different post-translational modifications (PTMs). The addition/removal of PTMs to α- or β-tubulins is catalyzed by specific enzymes and allows combinatory patterns largely enriching the distinct biochemical and biophysical properties of MTs, cre

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Antel, Matthew, Taylor Simao, Muhammed Burak Bener, and Mayu Inaba. "Drosophila CG17003/leaky (lky) is required for microtubule acetylation in early germ cells in Drosophila ovary." PLOS ONE 17, no. 11 (2022): e0276704. http://dx.doi.org/10.1371/journal.pone.0276704.

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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). α-tubulin K40 acetylation has been shown to stabilize microtubules via enhancing microtubule resilience against mechanical stress. Here we show that a previously uncharacterized αTAT, Drosophila CG17003/leaky (lky), is required for α-tubulin K40 acetylation in early germ cells in Drosophila ovary. We found that loss of lky resulted in a progressive egg chamber fusion phenotype accompanied with mislocalizatio

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6

Niu, Xiaoxiao, Chuan-Xi Mao, Shan Wang та ін. "α-Tubulin acetylation at lysine 40 regulates dendritic arborization and larval locomotion by promoting microtubule stability in Drosophila". PLOS ONE 18, № 2 (2023): e0280573. http://dx.doi.org/10.1371/journal.pone.0280573.

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Posttranslational modification of tubulin increases the dynamic complexity and functional diversity of microtubules. Acetylation of α-tubulin at Lys-40 is a highly conserved posttranslational modification that has been shown to improve the flexibility and resilience of microtubules. Here we studied the in vivo functions of α-tubulin acetylation by knocking-out Atat, the Drosophila α-tubulin acetyltransferase, and by mutating Lys-40 to Arg in α1-tubulin. We found a reduction in the dendritic arborization of larval class I dendritic arborization (da) neurons in both mutants. The dendritic develo

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7

Fernández-Barrera, Jaime, Miguel Bernabé-Rubio, Javier Casares-Arias та ін. "The actin-MRTF-SRF transcriptional circuit controls tubulin acetylation via α-TAT1 gene expression". Journal of Cell Biology 217, № 3 (2018): 929–44. http://dx.doi.org/10.1083/jcb.201702157.

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The role of formins in microtubules is not well understood. In this study, we have investigated the mechanism by which INF2, a formin mutated in degenerative renal and neurological hereditary disorders, controls microtubule acetylation. We found that silencing of INF2 in epithelial RPE-1 cells produced a dramatic drop in tubulin acetylation, increased the G-actin/F-actin ratio, and impaired myocardin-related transcription factor (MRTF)/serum response factor (SRF)–dependent transcription, which is known to be repressed by increased levels of G-actin. The effect on tubulin acetylation was caused

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8

Even, Aviel, Giovanni Morelli, Loïc Broix, et al. "ATAT1-enriched vesicles promote microtubule acetylation via axonal transport." Science Advances 5, no. 12 (2019): eaax2705. http://dx.doi.org/10.1126/sciadv.aax2705.

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Microtubules are polymerized dimers of α- and β-tubulin that underlie a broad range of cellular activities. Acetylation of α-tubulin by the acetyltransferase ATAT1 modulates microtubule dynamics and functions in neurons. However, it remains unclear how this enzyme acetylates microtubules over long distances in axons. Here, we show that loss of ATAT1 impairs axonal transport in neurons in vivo, and cell-free motility assays confirm a requirement of α-tubulin acetylation for proper bidirectional vesicular transport. Moreover, we demonstrate that the main cellular pool of ATAT1 is transported at

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9

Elesinnla, Abosede, Rehana Khatoon, Nicholas Kleinert, Junfang Wu, Jaylyn Waddell та Tibor Kristian. "Ethanol Administration in Mice Leads to Sex-Specific Changes in the Acetylation of α-Tubulin in the Cerebellum". Brain Sciences 15, № 4 (2025): 326. https://doi.org/10.3390/brainsci15040326.

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Background: Acetylation of α-tubulin is an important post-translational modification that helps maintain microtubules’ stability and dynamics, including axonal transport, cell signaling, and overall neuronal integrity. This study investigates sex-based differences in alcohol-induced acetylation of α-tubulin in mouse cerebellum. Methods: Adult, 3-month-old male and female C57BL/6 mice were administered 20% ethanol intraperitoneally. The cerebellum was dissected at 30 min, 1 h, 2 h, and 4 h post-injection. Expression levels of cerebellar acetylation of α-tubulin and enzymes mediating acetylation

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10

Olenieva, V. D., D. I. Lytvyn, A. I. Yemets, and Ya B. Blume. "Expression profiling of kinesins, involved in the development of autophagy in Arabidopsis thaliana, and the role of tubulin acetylation in the interaction of Atg8 protein with microtubules." Faktori eksperimental'noi evolucii organizmiv 22 (September 9, 2018): 162–68. http://dx.doi.org/10.7124/feeo.v22.942.

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Aim. To investigate the interrelation between changes in the expression levels of kinesin genes that are potentially involved in the development of stress-induced autophagy in Arabidopsis thaliana by means of microtubules, and the structural biology analysis of the role of α-tubulin acetylation in the regulation of interaction of α-tubulin with Atg8. Methods. The simulation of the influence of abiotic stresses. PCR analysis of changes in expression levels of kinesin genes. The molecular dynamics simulations of α-tubulin and Atg8 complexes were performed using the GROMACS 4.5.5 program. Results

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11

Sadoul, Karin, and Saadi Khochbin. "The growing landscape of tubulin acetylation: lysine 40 and many more." Biochemical Journal 473, no. 13 (2016): 1859–68. http://dx.doi.org/10.1042/bcj20160172.

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Tubulin heterodimers are the building block of microtubules, which are major elements of the cytoskeleton. Several types of post-translational modifications are found on tubulin subunits as well as on the microtubule polymer to regulate the multiple roles of microtubules. Acetylation of lysine 40 (K40) of the α-tubulin subunit is one of these post-translational modifications which has been extensively studied. We summarize the current knowledge about the structural aspects of K40 acetylation, the functional consequences, the enzymes involved and their regulation. Most importantly, we discuss t

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12

Tomas-Roig, Jordi, Shyam Ramasamy, Diana Zbarsky, Ursula Havemann-Reinecke та Sigrid Hoyer-Fender. "Psychosocial stress and cannabinoid drugs affect acetylation of α-tubulin (K40) and gene expression in the prefrontal cortex of adult mice". PLOS ONE 17, № 9 (2022): e0274352. http://dx.doi.org/10.1371/journal.pone.0274352.

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The dynamics of neuronal microtubules are essential for brain plasticity. Vesicular transport and synaptic transmission, additionally, requires acetylation of α-tubulin, and aberrant tubulin acetylation and neurobiological deficits are associated. Prolonged exposure to a stressor or consumption of drugs of abuse, like marihuana, lead to neurological changes and psychotic disorders. Here, we studied the effect of psychosocial stress and the administration of cannabinoid receptor type 1 drugs on α-tubulin acetylation in different brain regions of mice. We found significantly decreased tubulin ac

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13

Xie, Xi, Ruibao Ren, Bao yuan Zhang, and Ping Liu. "Suppression of Microtubule Acetylation Mediates Theanti-Leukemic Effect of CDK9 Inhibition." Blood 142, Supplement 1 (2023): 5772. http://dx.doi.org/10.1182/blood-2023-187901.

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Suppression of Microtubule Acetylation Mediates the Anti-Leukemic Effect of CDK9 Inhibition Xi Xie1, BaoyuanZhang1, Ping Liu1, Ruibao Ren1,2 1. Shanghai Institute of Hematology, State Key Laboratory for Medical Genomics, National Research Center for Translational Medicine at Shanghai, International Center for Aging and Cancer, Collaborative Innovation Center of Hematology, Ruijin Hospital affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China. 2. International Center for Aging and Cancer, Hainan Medical University, Haikou, Hainan Province, China. Cyclin-dependent kinas

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14

Aguilar, Andrea, Lars Becker, Thomas Tedeschi, Stefan Heller, Carlo Iomini та Maxence V. Nachury. "α-Tubulin K40 acetylation is required for contact inhibition of proliferation and cell–substrate adhesion". Molecular Biology of the Cell 25, № 12 (2014): 1854–66. http://dx.doi.org/10.1091/mbc.e13-10-0609.

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Acetylation of α-tubulin on lysine 40 marks long-lived microtubules in structures such as axons and cilia, and yet the physiological role of α-tubulin K40 acetylation is elusive. Although genetic ablation of the α-tubulin K40 acetyltransferase αTat1 in mice did not lead to detectable phenotypes in the developing animals, contact inhibition of proliferation and cell–substrate adhesion were significantly compromised in cultured αTat1−/− fibroblasts. First, αTat1−/− fibroblasts kept proliferating beyond the confluent monolayer stage. Congruently, αTat1−/− cells failed to activate Hippo signaling

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15

Kalebic, Nereo, Concepcion Martinez, Emerald Perlas та ін. "Tubulin Acetyltransferase αTAT1 Destabilizes Microtubules Independently of Its Acetylation Activity". Molecular and Cellular Biology 33, № 6 (2012): 1114–23. http://dx.doi.org/10.1128/mcb.01044-12.

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Acetylation of α-tubulin at lysine 40 (K40) is a well-conserved posttranslational modification that marks long-lived microtubules but has poorly understood functional significance. Recently, αTAT1, a member of the Gcn5-relatedN-acetyltransferase superfamily, has been identified as an α-tubulin acetyltransferase in ciliated organisms. Here, we explored the function of αTAT1 with the aim of understanding the consequences of αTAT1-mediated microtubule acetylation. We demonstrate that α-tubulin is the major target of αTAT1 but that αTAT1 also acetylates itself in a regulatory mechanism that is req

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16

Rahimi, Amir Mohammad, Mingfang Cai, Irem Kılıҫ, Zahra Basir Kazerouni, Constanza Tapia Contreras та Sigrid Hoyer-Fender. "Expression of α-Tubulin Acetyltransferase 1 and Tubulin Acetylation as Selective Forces in Cell Competition". Cells 10, № 2 (2021): 390. http://dx.doi.org/10.3390/cells10020390.

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The wound healing response of fibroblasts critically depends on the primary cilium, a sensory organelle protruding into the environment and comprising a stable axonemal structure. A characteristic marker for primary cilia is acetylation of axonemal tubulin. Although formation of primary cilia is under cell cycle control, the environmental cues affecting ciliation are not fully understood. Our purpose was, therefore, to study the impact of culture conditions on cilia formation in NIH3T3 fibroblasts. We quantified ciliation in different NIH3T3 sub-cell lines and culture conditions by immunodetec

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17

Dorsch, Schuldt, Remedios, et al. "Protein Quality Control Activation and Microtubule Remodeling in Hypertrophic Cardiomyopathy." Cells 8, no. 7 (2019): 741. http://dx.doi.org/10.3390/cells8070741.

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Hypertrophic cardiomyopathy (HCM) is the most common inherited cardiac disorder. It is mainly caused by mutations in genes encoding sarcomere proteins. Mutant forms of these highly abundant proteins likely stress the protein quality control (PQC) system of cardiomyocytes. The PQC system, together with a functional microtubule network, maintains proteostasis. We compared left ventricular (LV) tissue of nine donors (controls) with 38 sarcomere mutation-positive (HCMSMP) and 14 sarcomere mutation-negative (HCMSMN) patients to define HCM and mutation-specific changes in PQC. Mutations in HCMSMP re

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Aslan, Joseph E., Kevin G. Phillips, Laura D. Healy, Asako Itakura, Jiaqing Pang та Owen J. T. McCarty. "Histone deacetylase 6-mediated deacetylation of α-tubulin coordinates cytoskeletal and signaling events during platelet activation". American Journal of Physiology-Cell Physiology 305, № 12 (2013): C1230—C1239. http://dx.doi.org/10.1152/ajpcell.00053.2013.

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The tubulin cytoskeleton plays a key role in maintaining the characteristic quiescent discoid shape of resting platelets. Upon activation, platelets undergo a dramatic change in shape; however, little is known of how the microtubule system contributes to regulating platelet shape and function. Here we investigated the role of the covalent modification of α-tubulin by acetylation in the regulation of platelet physiology during activation. Superresolution microscopy analysis of the platelet tubulin cytoskeleton showed that the marginal band together with an interconnected web of finer tubulin st

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19

Othman, Ahmad, Marcus Winogradzki, Shreya Patel, Waddell Holmes, Alan Blank, and Jitesh Pratap. "The Role of Runx2 in Microtubule Acetylation in Bone Metastatic Breast Cancer Cells." Cancers 14, no. 14 (2022): 3436. http://dx.doi.org/10.3390/cancers14143436.

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Bone metastasis of breast cancer results in severe bone loss, fractures, and death. Crosstalk between breast cancer cells and bone resident cells promotes osteoclast activity and the release of growth factors from the bone matrix resulting in aggressive tumor growth and bone loss. We and others have shown that Runt-related transcription factor-2 (Runx2) promotes metastatic tumor growth-associated bone loss. Breast cancer cells also induce autophagy to survive metabolic stress at the metastatic site. Recently, we reported a Runx2-dependent increase in autophagy. In this study, to examine the un

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20

Labisso, Wajana, Ana-Caroline Raulin, Lucky Nwidu та ін. "The Loss of α- and β-Tubulin Proteins Are a Pathological Hallmark of Chronic Alcohol Consumption and Natural Brain Ageing". Brain Sciences 8, № 9 (2018): 175. http://dx.doi.org/10.3390/brainsci8090175.

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Repetitive excessive alcohol intoxication leads to neuronal damage and brain shrinkage. We examined cytoskeletal protein expression in human post-mortem tissue from Brodmann’s area 9 of the prefrontal cortex (PFC). Brain samples from 44 individuals were divided into equal groups of 11 control, 11 alcoholic, 11 non-alcoholic suicides, and 11 suicide alcoholics matched for age, sex, and post-mortem delay. Tissue from alcoholic cohorts displayed significantly reduced expression of α- and β-tubulins, and increased levels of acetylated α-tubulin. Protein levels of histone deacetylase-6 (HDAC6), and

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Coombes, Courtney, Ami Yamamoto, Mark McClellan та ін. "Mechanism of microtubule lumen entry for the α-tubulin acetyltransferase enzyme αTAT1". Proceedings of the National Academy of Sciences 113, № 46 (2016): E7176—E7184. http://dx.doi.org/10.1073/pnas.1605397113.

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Microtubules are structural polymers inside of cells that are subject to posttranslational modifications. These posttranslational modifications create functionally distinct subsets of microtubule networks in the cell, and acetylation is the only modification that takes place in the hollow lumen of the microtubule. Although it is known that the α-tubulin acetyltransferase (αTAT1) is the primary enzyme responsible for microtubule acetylation, the mechanism for how αTAT1 enters the microtubule lumen to access its acetylation sites is not well understood. By performing biochemical assays, fluoresc

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Liu, Pengfei, Shengwei Zhang, Jingyi Ma, Dongning Jin, Yali Qin та Mingzhou Chen. "Vimentin inhibits α-tubulin acetylation via enhancing α-TAT1 degradation to suppress the replication of human parainfluenza virus type 3". PLOS Pathogens 18, № 9 (2022): e1010856. http://dx.doi.org/10.1371/journal.ppat.1010856.

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We previously found that, among human parainfluenza virus type 3 (HPIV3) proteins, the interaction of nucleoprotein (N) and phosphoprotein (P) provides the minimal requirement for the formation of cytoplasmic inclusion bodies (IBs), which are sites of RNA synthesis, and that acetylated α-tubulin enhances IB fusion and viral replication. In this study, using immunoprecipitation and mass spectrometry assays, we determined that vimentin (VIM) specifically interacted with the N–P complex of HPIV3, and that the head domain of VIM was responsible for this interaction, contributing to the inhibition

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Yu, Jinyan, Zhongsen Ma, Sreerama Shetty, Mengshi Ma та Jian Fu. "Selective HDAC6 inhibition prevents TNF-α-induced lung endothelial cell barrier disruption and endotoxin-induced pulmonary edema". American Journal of Physiology-Lung Cellular and Molecular Physiology 311, № 1 (2016): L39—L47. http://dx.doi.org/10.1152/ajplung.00051.2016.

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Lung endothelial damage contributes to the pathogenesis of acute lung injury. New strategies against lung endothelial barrier dysfunction may provide therapeutic benefits against lung vascular injury. Cell-cell junctions and microtubule cytoskeleton are basic components in maintaining endothelial barrier integrity. HDAC6, a deacetylase primarily localized in the cytoplasm, has been reported to modulate nonnuclear protein function through deacetylation. Both α-tubulin and β-catenin are substrates for HDAC6. Here, we examined the effects of tubastatin A, a highly selective HDAC6 inhibitor, on TN

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Luo, J., S. Megee, and I. Dobrinski. "288 THE EXPRESSION PATTERN OF ACETYLATED ALPHA-TUBULIN IS CONSERVED IN PORCINE AND MURINE SPERMATOGONIAL STEM CELLS." Reproduction, Fertility and Development 20, no. 1 (2008): 223. http://dx.doi.org/10.1071/rdv20n1ab288.

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During mammalian spermatogenesis, spermatogonial stem cells (SSCs) reside in the stem cell niche on the basement membrane where they undergo self-renewing divisions. Differentiating daughter cells are located progressively more toward the tubular lumen where they ultimately form spermatozoa. The mechanisms responsible for maintenance of SSCs at the basement membrane are unclear. Microtubules consisting of α/β-tubulin heterodimers are associated with many cellular functions. Reversible acetylation of α-tubulin at Lys40 has been implicated in regulating microtubule stability and function. Acetyl

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Delgado, Inês L. S., João Gonçalves, Rita Fernandes, et al. "Balancing Act: Tubulin Glutamylation and Microtubule Dynamics in Toxoplasma gondii." Microorganisms 12, no. 3 (2024): 488. http://dx.doi.org/10.3390/microorganisms12030488.

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The success of the intracellular parasite Toxoplasma gondii in invading host cells relies on the apical complex, a specialized microtubule cytoskeleton structure associated with secretory organelles. The T. gondii genome encodes three isoforms of both α- and β-tubulin, which undergo specific post-translational modifications (PTMs), altering the biochemical and biophysical proprieties of microtubules and modulating their interaction with associated proteins. Tubulin PTMs represent a powerful and evolutionarily conserved mechanism for generating tubulin diversity, forming a biochemical ‘tubulin

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Shi, Lang, Zhixia Song, Chenglong Li, et al. "HDAC6 Inhibition Alleviates Ischemia- and Cisplatin-Induced Acute Kidney Injury by Promoting Autophagy." Cells 11, no. 24 (2022): 3951. http://dx.doi.org/10.3390/cells11243951.

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Histone deacetylase (HDAC) 6 exists exclusively in cytoplasm and deacetylates cytoplasmic proteins such as α-tubulin. HDAC6 dysfunction is associated with several pathological conditions in renal disorders, including UUO-induced fibrotic kidneys and rhabdomyolysis-induced nephropathy. However, the role of HDAC6 in ischemic acute kidney injury (AKI) and the mechanism by which HDAC6 inhibition protects tubular cells after AKI remain unclear. In the present study, we observed that HDAC6 was markedly activated in kidneys subjected to ischemia- and cisplatin (cis)-induced AKI treatment. Pharmacolog

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Creppe, Catherine, and Marcus Buschbeck. "Elongator: An Ancestral Complex Driving Transcription and Migration through Protein Acetylation." Journal of Biomedicine and Biotechnology 2011 (2011): 1–8. http://dx.doi.org/10.1155/2011/924898.

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Elongator is an evolutionary highly conserved complex. At least two of its cellular functions rely on the intrinsic lysine acetyl-transferase activity of the Elongator complex. Its two known substrates—Histone H3 and α-Tubulin—reflect the different roles of Elongator in the cytosol and the nucleus. A picture seems to emerge in which nuclear Elongator could regulate the transcriptional elongation of a subset of stress-inducible genes through acetylation of Histone H3 in the promoter-distal gene body. In the cytosol, Elongator-mediated acetylation of α-Tubulin contributes to intracellular traffi

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Sun, Wanwei, Xiaojian Ma, Heping Wang, et al. "MYO1F regulates antifungal immunity by regulating acetylation of microtubules." Proceedings of the National Academy of Sciences 118, no. 30 (2021): e2100230118. http://dx.doi.org/10.1073/pnas.2100230118.

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Opportunistic fungal infections have become one of the leading causes of death among immunocompromised patients, resulting in an estimated 1.5 million deaths each year worldwide. The molecular mechanisms that promote host defense against fungal infections remain elusive. Here, we find that Myosin IF (MYO1F), an unconventional myosin, promotes the expression of genes that are critical for antifungal innate immune signaling and proinflammatory responses. Mechanistically, MYO1F is required for dectin-induced α-tubulin acetylation, acting as an adaptor that recruits both the adaptor AP2A1 and α-tu

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Stoner, Michael W., Dharendra Thapa, Manling Zhang та ін. "α-Lipoic acid promotes α-tubulin hyperacetylation and blocks the turnover of mitochondria through mitophagy". Biochemical Journal 473, № 12 (2016): 1821–30. http://dx.doi.org/10.1042/bcj20160281.

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Lysine acetylation is tightly coupled to the nutritional status of the cell, as the availability of its cofactor, acetyl-CoA, fluctuates with changing metabolic conditions. Recent studies have demonstrated that acetyl-CoA levels act as an indicator of cellular nourishment, and increased abundance of this metabolite can block the induction of cellular recycling programmes. In the present study we investigated the cross-talk between mitochondrial metabolic pathways, acetylation and autophagy, using chemical inducers of mitochondrial acetyl-CoA production. Treatment of cells with α-lipoic acid (α

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Howes, Stuart C., Gregory M. Alushin, Toshinobu Shida, Maxence V. Nachury, and Eva Nogales. "Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure." Molecular Biology of the Cell 25, no. 2 (2014): 257–66. http://dx.doi.org/10.1091/mbc.e13-07-0387.

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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. Acetylation of Lys-40 on α-tubulin is unique in that it is located on the luminal surface of microtubules, away from the interaction sites of most MAPs and motors. We investigate whether acetylation alters the architecture of microtubules or the conformation of tubulin, using cryo–electron microscopy (cryo-EM). No significan

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Sharma, Chiranjeev, Yong Jin Oh, Byoungduck Park, et al. "Development of Thiazolidinedione-Based HDAC6 Inhibitors to Overcome Methamphetamine Addiction." International Journal of Molecular Sciences 20, no. 24 (2019): 6213. http://dx.doi.org/10.3390/ijms20246213.

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Thiazolidinedione is a five-membered heterocycle that is widely used in drug discovery endeavors. In this study, we report the design, synthesis, and biological evaluation of a series of thiazolidinedione-based HDAC6 inhibitors. In particular, compound 6b exerts an excellent inhibitory activity against HDAC6 with an IC50 value of 21 nM, displaying a good HDAC6 selectivity over HDAC1. Compound 6b dose-dependently induces the acetylation level of α-tubulin via inhibition of HDAC6 in human neuroblastoma SH-SY5Y cell line. Moreover, compound 6b efficiently reverses methamphetamine-induced morpholo

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Patel, Shreya, Marcus Winogradzki, Ahmad Othman, Waddell Holmes, and Jitesh Pratap. "Abstract 270: The novel control mechanism of the tubulin code and vesicular trafficking in breast cancer bone metastatic cells." Cancer Research 82, no. 12_Supplement (2022): 270. http://dx.doi.org/10.1158/1538-7445.am2022-270.

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Abstract Metastasis of breast cancer (BC) to bone results in severe bone loss, fractures, and death. The crosstalk between BC cells and bone resident cells dramatically increases osteoclast activity, resulting in the release of growth factors from the bone matrix that causes aggressive tumor growth and bone loss. A potentially important aspect of this process is vesicular trafficking on microtubules (MTs) which can affect the output of signaling pathways and secretory activity of metastatic bone cells. MTs are cytoskeletal filaments composed of heterodimers, α- and β-tubulin. The tubulin isoty

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Hu, Yi. "Post-translational modification of cytoskeleton regulates anti-tumor cytotoxicity in γδ T cells". Journal of Immunology 204, № 1_Supplement (2020): 88.19. http://dx.doi.org/10.4049/jimmunol.204.supp.88.19.

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Abstract γδ T cells based immunotherapy has emerged as a new treatment strategy for malignant tumors. The underlying cytotoxic mechanism against cancer cells involves surface receptor recognition molecules such as LFA-1, NKG2D, TRAIL, CD16, CD107a, and FasL, as well as cytokines such TNFα, IFNγ, perforin, and granzyme B. Previously, it has been shown that the cytoskeleton plays pivotal roles in T cell immunity. Nevertheless, the role of cytoskeleton in γδ T cell anti-tumor immunity remains largely unknown. In our work, we attempted to elucidate the functions of cytoskeleton in regulating the a

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Eshun-Wilson, Lisa, Rui Zhang, Didier Portran та ін. "Effects of α-tubulin acetylation on microtubule structure and stability". Proceedings of the National Academy of Sciences 116, № 21 (2019): 10366–71. http://dx.doi.org/10.1073/pnas.1900441116.

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Acetylation of K40 in α-tubulin is the sole posttranslational modification to mark the luminal surface of microtubules. It is still controversial whether its relationship with microtubule stabilization is correlative or causative. We have obtained high-resolution cryo-electron microscopy (cryo-EM) reconstructions of pure samples of αTAT1-acetylated and SIRT2-deacetylated microtubules to visualize the structural consequences of this modification and reveal its potential for influencing the larger assembly properties of microtubules. We modeled the conformational ensembles of the unmodified and

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Pongrakhananon, Varisa, Hiroko Saito, Sylvain Hiver, et al. "CAMSAP3 maintains neuronal polarity through regulation of microtubule stability." Proceedings of the National Academy of Sciences 115, no. 39 (2018): 9750–55. http://dx.doi.org/10.1073/pnas.1803875115.

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The molecular mechanisms that guide each neuron to become polarized, forming a single axon and multiple dendrites, remain unknown. Here we show that CAMSAP3 (calmodulin-regulated spectrin-associated protein 3), a protein that regulates the minus-end dynamics of microtubules, plays a key role in maintaining neuronal polarity. In mouse hippocampal neurons, CAMSAP3 was enriched in axons. Although axonal microtubules were generally acetylated, CAMSAP3 was preferentially localized along a less-acetylated fraction of the microtubules. CAMSAP3-mutated neurons often exhibited supernumerary axons, alon

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Solinger, Jachen A., Roberta Paolinelli, Holger Klöß та ін. "The Caenorhabditis elegans Elongator Complex Regulates Neuronal α-tubulin Acetylation". PLoS Genetics 6, № 1 (2010): e1000820. http://dx.doi.org/10.1371/journal.pgen.1000820.

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Kim, Byeong-Seong, Taegwan Yoon та Jee-Yin Ahn. "Id2 regulates α-tubulin acetylation by Sirt2, promoting axon growth". IBRO Reports 6 (вересень 2019): S471. http://dx.doi.org/10.1016/j.ibror.2019.07.1484.

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Valenzuela-Fernández, Agustín, Susana Álvarez, Mónica Gordon-Alonso, et al. "Histone Deacetylase 6 Regulates Human Immunodeficiency Virus Type 1 Infection." Molecular Biology of the Cell 16, no. 11 (2005): 5445–54. http://dx.doi.org/10.1091/mbc.e05-04-0354.

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Efficient human immunodeficiency virus (HIV)-1 infection depends on multiple interactions between the viral gp41/gp120 envelope (Env) proteins and cell surface receptors. However, cytoskeleton-associated proteins that modify membrane dynamics may also regulate the formation of the HIV-mediated fusion pore and hence viral infection. Because the effects of HDAC6-tubulin deacetylase on cortical α-tubulin regulate cell migration and immune synapse organization, we explored the possible role of HDAC6 in HIV-1-envelope-mediated cell fusion and infection. The binding of the gp120 protein to CD4+-perm

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Stemberger, Megan B., Julia A. Ju, Keyata N. Thompson та ін. "Hydrogen Peroxide Induces α-Tubulin Detyrosination and Acetylation and Impacts Breast Cancer Metastatic Phenotypes". Cells 12, № 9 (2023): 1266. http://dx.doi.org/10.3390/cells12091266.

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Levels of hydrogen peroxide are highly elevated in the breast tumor microenvironment compared to normal tissue. Production of hydrogen peroxide is implicated in the mechanism of action of many anticancer therapies. Several lines of evidence suggest hydrogen peroxide mediates breast carcinogenesis and metastasis, though the molecular mechanism remains poorly understood. This study elucidates the effects of exposure to elevated hydrogen peroxide on non-tumorigenic MCF10A mammary epithelial cells, tumorigenic MCF7 cells, and metastatic MDA-MB-231 breast cancer cells. Hydrogen peroxide treatment r

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Kim, Go-Woon, Lin Li, Mohammad Ghorbani, Linya You та Xiang-Jiao Yang. "Mice lacking α-tubulin acetyltransferase 1 are viable but display α-tubulin acetylation deficiency and dentate gyrus distortion." Journal of Biological Chemistry 291, № 48 (2016): 25279. http://dx.doi.org/10.1074/jbc.a113.464792.

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Kim, Go-Woon, Lin Li, Mohammad Gorbani, Linya You та Xiang-Jiao Yang. "Mice Lacking α-Tubulin Acetyltransferase 1 Are Viable but Display α-Tubulin Acetylation Deficiency and Dentate Gyrus Distortion". Journal of Biological Chemistry 288, № 28 (2013): 20334–50. http://dx.doi.org/10.1074/jbc.m113.464792.

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Adamakis, Ioannis-Dimosthenis S., Emmanuel Panteris, and Eleftherios P. Eleftheriou. "Tubulin Acetylation Mediates Bisphenol A Effects on the Microtubule Arrays of Allium cepa and Triticum turgidum." Biomolecules 9, no. 5 (2019): 185. http://dx.doi.org/10.3390/biom9050185.

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The effects of bisphenol A (BPA), a prevalent endocrine disruptor, on both interphase and mitotic microtubule array organization was examined by immunofluorescence microscopy in meristematic root cells of Triticum turgidum (durum wheat) and Allium cepa (onion). In interphase cells of A. cepa, BPA treatment resulted in substitution of cortical microtubules by annular/spiral tubulin structures, while in T. turgidum BPA induced cortical microtubule fragmentation. Immunolocalization of acetylated α-tubulin revealed that cortical microtubules of T. turgidum were highly acetylated, unlike those of A

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Carbajal, Agustín, María E. Chesta, C. Gastón Bisig, and Carlos A. Arce. "A novel method for purification of polymerizable tubulin with a high content of the acetylated isotype." Biochemical Journal 449, no. 3 (2013): 643–48. http://dx.doi.org/10.1042/bj20121439.

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Tubulin can be acetylated/deacetylated on Lys40 of the α-subunit. Studies of the post-translational acetylation/deacetylation of tubulin using biochemical techniques require tubulin preparations that are enriched in AcTubulin (acetylated tubulin) and (for comparison) preparations lacking AcTubulin. Assembly–disassembly cycling of microtubules gives tubulin preparations that contain little or no AcTubulin. In the present study we demonstrated that this result is owing to the presence of high deacetylating activity in the extracts. This deacetylating activity in rat brain homogenates was inhibit

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Qu, Pengxiang, Zhenzi Zuo, Zhengqing Liu та ін. "Sperm-borne small RNAs regulate α-tubulin acetylation and epigenetic modification of early bovine somatic cell nuclear transfer embryos". Molecular Human Reproduction 25, № 8 (2019): 471–82. http://dx.doi.org/10.1093/molehr/gaz023.

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AbstractAccumulated evidence indicates that sperm-borne small RNA plays a crucial role in embryonic development, especially the absence of the sperm-borne small RNA might be a major cause of the abnormal development of cloned embryos. In this study, we found that sperm-borne small RNA can affect abnormal pronuclear-like structures, postpone the timing of first embryo cleavage and enhance developmental competence of bovine somatic cell nuclear transfer (SCNT) embryos. In addition, the supplementation of sperm-borne small RNA can significantly increase live birth rates and decrease the birth wei

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Ryu, Na Mi, та Jung Min Kim. "The role of the α-tubulin acetyltransferase αTAT1 in the DNA damage response". Journal of Cell Science 133, № 17 (2020): jcs246702. http://dx.doi.org/10.1242/jcs.246702.

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ABSTRACTLysine 40 acetylation of α-tubulin (Ac-α-tubulin), catalyzed by the acetyltransferase αTAT1, marks stabilized microtubules. Recently, there is growing evidence to suggest crosstalk between the DNA damage response (DDR) and microtubule organization; we therefore investigated whether αTAT1 is involved in the DDR. Following treatment with DNA-damaging agents, increased levels of Ac-α-tubulin were detected. We also observed significant induction of Ac-α-tubulin after depletion of DNA repair proteins, suggesting that αTAT1 is positively regulated in response to DNA damage. Intriguingly, αTA

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Santo, Loredana, Teru Hideshima, Andrew L. Kung, et al. "Pharmacodynamic and Pharmacokinetic Properties of a Novel and Selective HDAC6 Inhibitor, ACY-1215, in Combination with Bortezomib in Multiple Myeloma." Blood 118, no. 21 (2011): 2912. http://dx.doi.org/10.1182/blood.v118.21.2912.2912.

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Abstract Abstract 2912 HDAC enzymes are being studied as novel therapeutic targets in several cancers including multiple myeloma (MM). In particular, the combination of proteasome inhibitors (e.g. bortezomib (BZ)) with Histone Deacetylase (HDAC) inhibitors have shown very promising results in pre-clinical MM models. HDAC6, a Class II HDAC, has been linked to the activity of aggresomes that degrade unfolded and misfolded ubiquitinated proteins. Targeting both proteasomal and aggresomal protein degradation systems with proteasome inhibitors and HDAC inhibitors, respectively, induces accumulation

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Read, M., T. Sherwin, S. P. Holloway, K. Gull, and J. E. Hyde. "Microtubular organization visualized by immunofluorescence microscopy during erythrocytic schizogony in Plasmodium falciparum and investigation of post-translational modifications of parasite tubulin." Parasitology 106, no. 3 (1993): 223–32. http://dx.doi.org/10.1017/s0031182000075041.

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SUMMARYWe describe a novel procedure for the immunofluorescent investigation of Plasmodium falciparum. This has allowed us to visualize clearly microtubular structures and their changing conformation through the erythrocytic cell-cycle, to the stage of cytodifferentiation leading to merozoite release. The images of spindle development we observed, together with an analysis of nuclear body numbers in large numbers of parasites, indicate that there is an apparent asynchrony in chromosomal multiplication within a single parasite. Using antibodies specific for post-translational modification of α-

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Cueva, Juan G., Jen Hsin, Kerwyn Casey Huang та Miriam B. Goodman. "Posttranslational Acetylation of α-Tubulin Constrains Protofilament Number in Native Microtubules". Current Biology 22, № 12 (2012): 1066–74. http://dx.doi.org/10.1016/j.cub.2012.05.012.

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Ohkawa, Noriaki, Shunichiro Sugisaki, Eri Tokunaga, Kazuko Fujitani, Mitsutoshi Setou та Kaoru Inokuchi. "ARD1-NAT1 complex regulates neuronal dendritic arborization through α-tubulin acetylation". Neuroscience Research 58 (січень 2007): S88. http://dx.doi.org/10.1016/j.neures.2007.06.1080.

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Li, Wande, Yinzhi Zhao та Iih-Nan Chou. "Nickel (Ni2+) Enhancement of α-Tubulin Acetylation in Cultured 3T3 Cells". Toxicology and Applied Pharmacology 140, № 2 (1996): 461–70. http://dx.doi.org/10.1006/taap.1996.0243.

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