Academic literature on the topic 'Acetylated α-tubulin'
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Journal articles on the topic "Acetylated α-tubulin"
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Alonso, Victoria Lucia, Gabriela Vanina Villanova, Carla Ritagliati, María Cristina Machado Motta, Pamela Cribb, and Esteban Carlos Serra. "Trypanosoma cruzi Bromodomain Factor 3 Binds Acetylated α-Tubulin and Concentrates in the Flagellum during Metacyclogenesis." Eukaryotic Cell 13, no. 6 (April 18, 2014): 822–31. http://dx.doi.org/10.1128/ec.00341-13.
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ABSTRACTBromodomains are highly conserved acetyl-lysine binding domains found mainly in proteins associated with chromatin and nuclear acetyltransferases. TheTrypanosoma cruzigenome encodes at least four bromodomain factors (TcBDFs). We describe here bromodomain factor 3 (TcBDF3), a bromodomain-containing protein localized in the cytoplasm.TcBDF3 cytolocalization was determined, using purified antibodies, by Western blot and immunofluorescence analyses in all life cycle stages ofT. cruzi. In epimastigotes and amastigotes, it was detected in the cytoplasm, the flagellum, and the flagellar pocket, and in trypomastigotes only in the flagellum. Subcellular localization ofTcBDF3 was also determined by digitonin extraction, ultrastructural immunocytochemistry, and expression ofTcBDF3 fused to cyan fluorescent protein (CFP). Tubulin can acquire different posttranslational modifications, which modulate microtubule functions. Acetylated α-tubulin has been found in the axonemes of flagella and cilia, as well as in the subpellicular microtubules of trypanosomatids.TcBDF3 and acetylated α-tubulin partially colocalized in isolated cytoskeletons and flagella fromT. cruziepimastigotes and trypomastigotes. Interaction between the two proteins was confirmed by coimmunoprecipitation and far-Western blot assays with synthetic acetylated α-tubulin peptides and recombinantTcBDF3.
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HARRISON, ALISTAIR, HOWARD STEBBINGS, and JEREMY S. HYAMS. "Different Patterns of α-Tubulin Post-Translational Modification in Ovarian Nutritive Tubes of Two Hemipteran Insects." Journal of Cell Science 100, no. 3 (November 1, 1991): 501–7. http://dx.doi.org/10.1242/jcs.100.3.501.
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Usage of the tyrosinated, detyrosinated and acetylated forms of α-tubulin in ovarian nutritive tube microtubules of the hemipterans Oncopeltus fasciatus and Notonecta glauca glauca was investigated by immunofluorescence microscopy of frozen sections of ovarioles with isotype-specific antibodies. In Oncopeltus, nutritive tubes at all stages of development contained tyrosinated α-tubulin and showed only a weak reaction to antibodies to the detyrosinated and acetylated forms. In Notonecta, tyrosinated α-tubulin was confined to a zone around the periphery of functional nutritive tubes; the body of these tubes, and the older, redundant, nutritive tubes stained strongly for both the detyrosinated and acetylated isotypes. The difference in isotype usage between the two species was confirmed by immunoblotting of 2-D gels of ovariole extracts. The results are consistent with the different time-course of oogenesis, and hence the longevity of the nutritive tube microtubules, in the two insects. A model for the insertion of new microtubules into nutritive tubes as they grow is proposed.
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Dorsch, Schuldt, Remedios, Schinkel, Jong, Michels, Kuster, Brundel, and Velden. "Protein Quality Control Activation and Microtubule Remodeling in Hypertrophic Cardiomyopathy." Cells 8, no. 7 (July 18, 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 result in poison polypeptides or reduced protein levels (haploinsufficiency, HI). The main findings were 1) several key PQC players were more abundant in HCM compared to controls, 2) after correction for sex and age, stabilizing heat shock protein (HSP)B1, and refolding, HSPD1 and HSPA2 were increased in HCMSMP compared to controls, 3) α-tubulin and acetylated α-tubulin levels were higher in HCM compared to controls, especially in HCMHI, 4) myosin-binding protein-C (cMyBP-C) levels were inversely correlated with α-tubulin, and 5) α-tubulin levels correlated with acetylated α-tubulin and HSPs. Overall, carrying a mutation affects PQC and α-tubulin acetylation. The haploinsufficiency of cMyBP-C may trigger HSPs and α-tubulin acetylation. Our study indicates that proliferation of the microtubular network may represent a novel pathomechanism in cMyBP-C haploinsufficiency-mediated HCM.
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Labisso, Wajana, Ana-Caroline Raulin, Lucky Nwidu, Artur Kocon, Declan Wayne, Amaia Erdozain, Benito Morentin, et al. "The Loss of α- and β-Tubulin Proteins Are a Pathological Hallmark of Chronic Alcohol Consumption and Natural Brain Ageing." Brain Sciences 8, no. 9 (September 11, 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 the microtubule-associated proteins MAP-2 and MAP-tau were reduced in alcoholic cohorts, although for MAPs this was not significant. Tubulin gene expressions increased in alcoholic cohorts but not significantly. Brains from rats administered alcohol for 4 weeks also displayed significantly reduced tubulin protein levels and increased α-tubulin acetylation. PFC tissue from control subjects had reduced tubulin protein expression that was most notable from the sixth to the eighth decade of life. Collectively, loss of neuronal tubulin proteins are a hallmark of both chronic alcohol consumption and natural brain ageing. The reduction of cytosolic tubulin proteins could contribute to the brain volumetric losses reported for alcoholic patients and the elderly.
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Luo, Jinping, Jose Rafael Rodriguez-Sosa, Lin Tang, Alla Bondareva, Susan Megee, and Ina Dobrinski. "Expression pattern of acetylated α-tubulin in porcine spermatogonia." Molecular Reproduction and Development 77, no. 4 (December 30, 2009): 348–52. http://dx.doi.org/10.1002/mrd.21153.
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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 (July 15, 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 underlying mechanisms of metastasis and tumor resistance to stress, we used a bone metastatic isogenic variant of breast cancer MDA-MB-231 cells isolated from a xenograft tumor mouse model of metastasis. Our results with immunofluorescence and biochemical approaches revealed that Runx2 promotes microtubule (MT) stability to facilitate autophagy. Stable MTs are critical for autophagosome trafficking and display increased acetylation at Lysine 40 of α-tubulin. Runx2 silencing decreases acetylated α-tubulin levels. The expression levels of HDAC6 and αTAT1, which serve to regulate the acetylation of α-tubulin, were not altered with Runx2 silencing. We found that HDAC6 interaction with α-tubulin is inhibited by Runt-related factor-2 (Runx2). We show that the expression of wild-type Runx2 can restore the acetylated polymer of MTs in Runx2 knockdown cells, while the C-terminal deletion mutant fails to rescue the polymer of MTs. Importantly, cellular stress, such as glucose starvation also increases the acetylation of α-tubulin. We found that the loss of Runx2 increases the sensitivity of breast cancer cells to MT-targeting agents. Overall, our results indicate a novel regulatory mechanism of microtubule acetylation and suggest that Runx2 and acetylated microtubules may serve as therapeutic targets for bone metastatic tumors.
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Denduluri, N., J. J. Lee, J. M. Walshe, S. X. Yang, U. Vatas, C. K. Chow, S. M. Steinberg, M. C. Cox, J. A. Low, and S. M. Swain. "Phase II clinical trial of ixabepilone in metastatic breast cancer (MBC) patients previously untreated with taxanes." Journal of Clinical Oncology 24, no. 18_suppl (June 20, 2006): 651. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.651.
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651 Background: Ixabepilone, an epothilone B analog, stabilizes microtubules by binding to tubulin. The response rate (RR) in taxane-pretreated patients at our institution was 22%. Methods: Patients (pts) were eligible if they had MBC previously untreated with taxanes and measurable disease by RECIST criteria. Ixabepilone was given at 6mg/m2/d intravenously days 1–5 every 3 weeks until unacceptable toxicity or disease progression. Primary objectives included RR and toxicity. Pts underwent pre and/or post treatment tumor biopsies for correlative studies. Acetylated α-tubulin, Tau-1, and p53 were stained with anti-acetylated α-tubulin, anti-Tau-1, and anti-p53 antibodies in samples from 13 pts. Staining was scored quantitatively using the Automated Cellular Imaging System. Results: Twenty-three pts received 197 cycles (C). Median of 7C (range 2–22) per pt were administered. Median age was 55 (range 22–79). Seven pts received 1 prior metastatic chemotherapy regimen. Ten of 23 or 43% (exact 95% confidence interval: 23.2% to 65.5%) pts had partial responses (PR), 9 (39%) stable disease (SD) (2 unconfirmed PRs), and 4 (17%) progressive disease (PD). Median time to progression was 5.3 months; median duration of response was 5.4 months from date of best response. Four pts required dose reductions for neutropenia, neuropathy or fatigue. Grade 3/4 toxicities included neutropenia (22%), fatigue (13%), anorexia (9%), infection without neutropenia (9%), motor neuropathy (4%), and muscle weakness (4%). No grade 3/4 sensory neuropathy was seen, but 35% and 13% of pts had grades 1 and 2 neuropathy respectively. Median acetylated α-tubulin at baseline was 0.2 in responders and 17.6 in non-responders (p=0.069). There were no differences in response according to Tau-1 or p53 expression at baseline. Conclusion: Ixabepilone is an effective treatment for MBC with a 43% RR in 23 pts previously untreated with taxanes. There was minimal hematologic toxicity and no grade 3 sensory neuropathy. The use of baseline level of acetylated α-tubulin to predict response may warrant further study. No significant financial relationships to disclose.
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Yang, Wulin, Xiangxiang Guo, Shermaine Thein, Feng Xu, Shigeki Sugii, Peter W. Baas, George K. Radda, and Weiping Han. "Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of α-tubulin." Biochemical Journal 449, no. 3 (January 9, 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 acetyltransferase MEC-17 and deacetylases SIRT2 (Sirtuin 2) and HDAC6 (histone deacetylase 6). Adipocyte development is inhibited in MEC-17-knockdown cells, but enhanced in MEC-17-overexpressing cells. Finally, we show that katanin, a microtubule-severing protein with enhanced activity on acetylated α-tubulin, is actively involved in adipogenesis. We propose that co-ordinated up-regulation of α-tubulin acetylation initiates cytoskeleton remodelling by promoting α-tubulin severing by katanin which, in turn, allows expansion of lipid droplets and accelerates the morphological transition toward mature adipocytes.
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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 (May 11, 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. cepa. In addition, elevation of tubulin acetylation by trichostatin A in A. cepa resulted in microtubule disruption similar to that observed in T. turgidum. BPA also disrupted all mitotic microtubule arrays in both species. It is also worth noting that mitotic microtubule arrays were acetylated in both plants. As assessed by BPA removal, its effects are reversible. Furthermore, taxol-stabilized microtubules were resistant to BPA, while recovery from oryzalin treatment in BPA solution resulted in the formation of ring-like tubulin conformations. Overall, these findings indicate the following: (1) BPA affects plant mitosis/cytokinesis by disrupting microtubule organization. (2) Microtubule disassembly probably results from impairment of free tubulin subunit polymerization. (3) The differences in cortical microtubule responses to BPA among the species studied are correlated to the degree of tubulin acetylation.
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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 (January 9, 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 inhibited by TSA (Trichostatin A) and tubacin, but not by nicotinamide, indicating that HDAC6 (histone deacetylase 6) is involved. TSA showed no effect on microtubule polymerization or depolymerization. We utilized these properties of TSA to prevent deacetylation during the assembly–disassembly procedure. The effective inhibitory concentration of TSA was 3 μM in the homogenate and 1 μM in the subsequent cycling steps. By comparison with immunopurified AcTubulin, we estimated that ~64% of the tubulin molecules in the three cycled preparations were acetylated. The protein profiles of these tubulin preparations, as assessed by SDS/PAGE and Coomassie Blue staining, were identical to that of a preparation completely lacking AcTubulin obtained by assembly–disassembly cycles in the absence of TSA. The tyrosination state and in vitro assembly–disassembly kinetics were the same regardless of the degree of acetylation.
Dissertations / Theses on the topic "Acetylated α-tubulin"
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Landucci, Elisa. "Modeling Rett syndrome with iPSCs-derived neurons." Doctoral thesis, Università di Siena, 2018. http://hdl.handle.net/11365/1051069.
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Rett syndrome is a severe neurodevelopmental disorder. The condition affects approximately one in every 10.000 females and is only rarely seen in males. Causative mutations in the transcriptional regulator MeCP2 have been identified in more than 95% of classic Rett patients; mutations in CDKL5 are responsible for the early onset seizures Rett variant and mutations in FOXG1 gene lead to the congenital Rett variant. To shed light on molecular mechanisms underlying Rett syndrome onset and progression in disease-relevant cells, we took advantage of the breakthrough genetic reprogramming technology and we investigated changes in iPSC-derived neurons from patients with different MECP2 and FOXG1 mutations and in the brain of Foxg1+/- mice. In total brains from Foxg1+/ − mutants we noticed a statistically significant overexpression of a group of neuropeptides expressed in the basal ganglia, cortex, hippocampus and hypothalamus: Oxytocin (Oxt), Arginine vasopressin (Avp) and Neuronatin (Nnat).Moreover, in iPSC-derived neuronal precursors and neurons mutated in FOXG1 and in Foxg1+/− mouse embryonic brain (E11.5) compared to wild type controls we found an increase in the expression of GluD1 and inhibitory synaptic markers, such as GAD67 and GABA AR-α1 and a decreased expression of excitatory synaptic markers, such as VGLUT1, GluA1, GluN1 and PSD-95, suggesting an excitation/inhibition imbalance in the developing brain of the congenital RTT variant. Furthermore, we investigated transcriptome changes in neurons differentiated from MECP2 mutated iPSC-derived neurons and we noticed a prominent GABAergic circuit disruption and a perturbation of cytoskeleton dynamics. In particular, in MECP2-mutated neurons we identified a significant decrease of acetylated α-tubulin which can be reverted by treatment with a selective inhibitor of HDAC6, the main α-tubulin deacetylase.
Taken togheter, these findings contribute to shed light on Rett pathogenic mechanisms and provide hints for the definition of new therapeutic strategies for Rett syndrome.
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Bílková, Karolína. "Vliv suplementace karotenoidy a oxidačního stresu na morfologii, kvalitu spermií a spermatogenezi u zebřičky pestré." Master's thesis, 2018. http://www.nusl.cz/ntk/nusl-380194.
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The phenotype-linked fertility hypothesis predicts that both, male carotenoid-based sexual ornamentation and their spermatozoa are phenotypically plastic and may be co-affected by the environment. One of the factors affecting their phenotype may be oxidative stress and the ability of organism to eliminate its effect. Oxidative stress may reduce sperm quality because sperm lack the ability to repair DNA, but it can also affect spermatogenesis itself. However, some substances may function as antioxidants, and thus eliminate effect of reactive oxygen species (oxidative stress) in the body. In this study, adult zebra finch males (Taeniopygia guttata) originating from the domesticated and recently wild-derived populations were exposed to the diquat (D), which enhances the oxidative stress, and carotenoid lutein (L), which could have an antioxidant function. Experimental design had factorial character 2x2 with a control (group L, D, LD, control). Neither oxidative stress, carotenoids, nor their interactions affected sperm morphology or velocity and it also did not increase abnormal sperm proportion in the ejaculate. However, the differences were observed at the molecular level, where by inducing the oxidative stress, the sperm had reduced signal intensity of acetylated α-tubulin in the sperm tails....
Book chapters on the topic "Acetylated α-tubulin"
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LeDizet, Michel, and Gianni Piperno. "[23] Detection of acetylated α-tubulin by specific antibodies." In Methods in Enzymology, 264–74. Elsevier, 1991. http://dx.doi.org/10.1016/0076-6879(91)96025-m.
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