Broader implications: biological and clinical significance of microtubule acetylation

References

• Chen S, Owens GC, Makarenkova H, Edelman DB. HDAC6 regulates mitochondrial transport in hippocampal neurons. PloS One. 2010;5(5):e10848.
   PubMed Web of Science ®Google Scholar
• Williams KA, Zhang M, Xiang S, et al. Extracellular signal-regulated kinase (ERK) phosphorylates histone deacetylase 6 (HDAC6) at serine 1035 to stimulate cell migration. J Bio Chem. 2013;288(46):33156–33170.
   PubMed Web of Science ®Google Scholar
• Bulinski JC, Gundersen GG. Stabilization of post-translational modification of microtubules during cellular morphogenesis. BioEssays News Rev Mol Cell Dev Biol. 1991;13(6):285–293.
   Google Scholar
• Janke C, Bulinski JC. Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions. Nat Rev Mol Cell Biol. 2011;12(12):773–786.
   PubMed Web of Science ®Google Scholar
• Dompierre JP, Godin JD, Charrin BC, et al. Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington’s disease by increasing tubulin acetylation. J Neurosci. 2007;27(13):3571–3583.
   PubMed Web of Science ®Google Scholar
• Reed NA, Cai D, Blasius TL, et al. Microtubule acetylation promotes kinesin-1 binding and transport. Curr Biol. 2006;16(21):2166–2172.
   Web of Science ®Google Scholar
• Chu C-W, Hou F, Zhang J, et al. A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation. Mol Biol Cell. 2011;22(4):448–456.
   Web of Science ®Google Scholar
• Piperno G, LeDizet M, Chang XJ. Microtubules containing acetylated alpha-tubulin in mammalian cells in culture. J Cell Biol. 1987;104(2):289–302.
   PubMed Web of Science ®Google Scholar
• Takemura R, Okabe S, Umeyama T, Kanai Y, Cowan NJ, Hirokawa N. Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau. J Cell Sci. 1992;103(Pt 4):953–964.
   PubMed Web of Science ®Google Scholar
• Nogales E, Whittaker M, Milligan RA, Downing KH. High-resolution model of the microtubule. Cell. 1999;96(1):79–88.
   Web of Science ®Google Scholar
• Howes SC, Alushin GM, Shida T, Nachury MV, Nogales E. Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure. Mol Biol Cell. 2014;25(2):257–266.
   Web of Science ®Google Scholar
• Soppina V, Herbstman JF, Skiniotis G, Verhey KJ. Luminal localization of α-tubulin K40 acetylation by cryo-EM analysis of fab-labeled microtubules. PloS One. 2012;7(10):e48204.
   Web of Science ®Google Scholar
• Greer K, Maruta H, L’Hernault SW, Rosenbaum JL. Alpha-tubulin acetylase activity in isolated Chlamydomonas flagella. J Cell Biol. 1985;101(6):2081–2084.
   Web of Science ®Google Scholar
• Tassara M, Döhner K, Brossart P, et al. Valproic acid in combination with all-trans retinoic acid and intensive therapy for acute myeloid leukemia in older patients. Blood. 2014;123(26):4027–4036.
   PubMed Web of Science ®Google Scholar
• Monastyrska I, Rieter E, Klionsky DJ, Reggiori F. Multiple roles of the cytoskeleton in autophagy. Biol Rev Camb Philos Soc. 2009;84(3):431–448.
   PubMed Web of Science ®Google Scholar
• Rymut SM, Harker A, Corey DA, et al. Reduced microtubule acetylation in cystic fibrosis epithelial cells. Am J Physiol Lung Cell Mol Physiol. 2013;305(6):L419–L431.
   Web of Science ®Google Scholar
• Dasmahapatra G, Patel H, Friedberg J, Quayle SN, Jones SS, Grant S. In vitro and in vivo interactions between the HDAC6 inhibitor ricolinostat (ACY1215) and the irreversible proteasome inhibitor carfilzomib in non-hodgkin lymphoma cells. Mol Cancer Ther. 2014;13(12):2886–2897.
   PubMed Web of Science ®Google Scholar
• Nahhas F, Dryden SC, Abrams J, Tainsky MA. Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin. Mol Cel. Biochem. 2007;303(1–2):221–230.
   Web of Science ®Google Scholar
• Steczkiewicz K, Kinch L, Grishin NV, Rychlewski L, Ginalski K. Eukaryotic domain of unknown function DUF738 belongs to Gcn5-related N-acetyltransferase superfamily. Cell Cycle. 2006;5(24):2927–2930.
   PubMed Web of Science ®Google Scholar
• Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R. Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. Proc Natl Acad Sci U S A. 2012;109(48):19655–19660.
   PubMed Web of Science ®Google Scholar
• Taschner M, Vetter M, Lorentzen E. Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA. Proc Natl Acad Sci U S A. 2012;109(48):19649–19654.
   Web of Science ®Google Scholar
• Kim G-W, Li L, Gorbani M, You L, Yang X-J. Mice lacking α-tubulin acetyltransferase 1 are viable but display α-tubulin acetylation deficiency and dentate gyrus distortion. J Biol Chem. 2013;288(28):20334–20350.
   PubMed Web of Science ®Google Scholar
• Aguilar A, Becker L, Tedeschi T, Heller S, Iomini C, Nachury MV. α-tubulin K40 acetylation is required for contact inhibition of proliferation and cell-substrate adhesion. Mol Biol Cell. 2014;25(12):1854–1866.
   PubMed Web of Science ®Google Scholar
• Li L, Wei D, Wang Q, et al. MEC-17 deficiency leads to reduced α-tubulin acetylation and impaired migration of cortical neurons. J Neurosci. 2012;32(37):12673–12683.
   PubMed Web of Science ®Google Scholar
• Hubbert C, Guardiola A, Shao R, et al. HDAC6 is a microtubule-associated deacetylase. Nature. 2002;417(6887):455–458.
   PubMed Web of Science ®Google Scholar
• Liu Y, Peng L, Seto E, Huang S, Qiu Y. Modulation of histone deacetylase 6 (HDAC6) nuclear import and tubulin deacetylase activity through acetylation. J Biol Chem. 2012;287(34):29168–29174.
   PubMed Web of Science ®Google Scholar
• Valenzuela-Fernández A, Cabrero JR, Serrador JM, Sánchez-Madrid F. HDAC6: a key regulator of cytoskeleton, cell migration and cell-cell interactions. Trends Cell Biol. 2008;18(6):291–297.
   PubMed Web of Science ®Google Scholar
• Schofield AV, Gamell C, Suryadinata R, Sarcevic B, Bernard O. Tubulin polymerization promoting protein 1 (Tppp1) phosphorylation by Rho-associated coiled-coil kinase (rock) and cyclin-dependent kinase 1 (Cdk1) inhibits microtubule dynamics to increase cell proliferation. J Biol Chem. 2013;288(11):7907–7917.
   PubMed Web of Science ®Google Scholar
• Zhang Y, Kwon S, Yamaguchi T, et al. Mice lacking histone deacetylase 6 have hyperacetylated tubulin but are viable and develop normally. Mol Cell Biol. 2008;28(5):1688–1701.
   PubMed Web of Science ®Google Scholar
• Jing E, Gesta S, Kahn CR. SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab. 2007;6(2):105–114.
   PubMed Web of Science ®Google Scholar
• Wang F, Nguyen M, Qin FX-F, Tong Q. SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell. 2007;6(4):505–514.
   PubMed Web of Science ®Google Scholar
• North BJ, Marshall BL, Borra MT, Denu JM, Verdin E. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell. 2003;11(2):437–444.
   PubMed Web of Science ®Google Scholar
• Pandithage R, Lilischkis R, Harting K, et al. The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility. J Cell Biol. 2008;180(5):915–929.
   Web of Science ®Google Scholar
• Inoue T, Hiratsuka M, Osaki M, et al. SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress. Oncogene. 2007;26(7):945–957.
   PubMed Web of Science ®Google Scholar
• Maxwell MM, Tomkinson EM, Nobles J, et al. The sirtuin 2 microtubule deacetylase is an abundant neuronal protein that accumulates in the aging CNS. Hum Mol Genet. 2011;20(20):3986–3996.
   PubMed Web of Science ®Google Scholar
• Kim H-S, Vassilopoulos A, Wang R-H, et al. SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity. Cancer Cell. 2011;20(4):487–499.
   PubMed Web of Science ®Google Scholar
• Bulinski JC. Microtubule modification: acetylation speeds anterograde traffic flow. Curr Biol. 2007;17(1):R18–R20.
   Web of Science ®Google Scholar
• Misawa T, Takahama M, Kozaki T, et al. Microtubule-driven spatial arrangement of mitochondria promotes activation of the NLRP3 inflammasome. Nat Immunol. 2013;14(5):454–460.
   PubMed Web of Science ®Google Scholar
• Winklhofer KF, Haass C. Mitochondrial dysfunction in Parkinson’s disease. Biochim Biophys Acta. 2010;1802(1):29–44.
   PubMed Web of Science ®Google Scholar
• Valdivieso AG, Clauzure M, Marín MC, et al. The mitochondrial complex I activity is reduced in cells with impaired cystic fibrosis transmembrane conductance regulator (CFTR) function. PloS One. 2012;7(11):e48059.
   Web of Science ®Google Scholar
• Gundersen GG, Bulinski JC. Distribution of tyrosinated and nontyrosinated alpha-tubulin during mitosis. J Cell Biol. 1986;102(3):1118–1126.
   Web of Science ®Google Scholar
• Wolf KW, Spanel-Borowski K. Acetylation of alpha-tubilin in different bovine cell types: implications for microtubule dynamics in interphase and mitosis. Cell Biol Int. 1995;19(1):43–52.
   Web of Science ®Google Scholar
• Asthana J, Kuchibhatla A, Jana SC, Ray K, Panda D. Dynein light chain 1 (LC8) association enhances microtubule stability and promotes microtubule bundling. J Biol Chem. 2012;287(48):40793–40805.
   Web of Science ®Google Scholar
• Giustiniani J, Couloubaly S, Baillet A, et al. Basal endothelial nitric oxide synthase (eNOS) phosphorylation on Ser(1177) occurs in a stable microtubule- and tubulin acetylation-dependent manner. Exp Cell Res. 2009;315(20):3509–3520.
   Web of Science ®Google Scholar
• Mattila JT, Thomas AC. Nitric oxide synthase: non-canonical expression patterns. Front Immunol. 2014;5:478.
   PubMed Web of Science ®Google Scholar
• Kim SR, Kim DI, Kim SH, et al. NLRP3 inflammasome activation by mitochondrial ROS in bronchial epithelial cells is required for allergic inflammation. Cell Death Dis. 2014;5:e1498.
   PubMed Web of Science ®Google Scholar
• McGettrick AF, O’Neill LAJ. How metabolism generates signals during innate immunity and inflammation. J Biol Chem. 2013;288(32):22893–22898.
   PubMed Web of Science ®Google Scholar
• Shida T, Cueva JG, Xu Z, Goodman MB, Nachury MV. The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc Natl Acad Sci U S A. 2010;107(50):21517–21522.
   PubMed Web of Science ®Google Scholar
• Wang B, Rao Y-H, Inoue M, et al. Microtubule acetylation amplifies p38 kinase signalling and anti-inflammatory IL-10 production. Nat Commun. 2014;5:3479.
   PubMed Web of Science ®Google Scholar
• Glenner GG, Wong CW. Alzheimer’s disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun. 1984;120(3):885–890.
   PubMed Web of Science ®Google Scholar
• Goedert M, Spillantini MG, Cairns NJ, Crowther RA. Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron. 1992;8(1):159–168.
   PubMed Web of Science ®Google Scholar
• Hyman BT, Van Hoesen GW, Damasio AR, Barnes CL. Alzheimer’s disease: cell-specific pathology isolates the hippocampal formation. Science. 1984;225(4667):1168–1170.
   PubMed Web of Science ®Google Scholar
• Masliah E, Hansen L, Albright T, Mallory M, Terry RD. Immunoelectron microscopic study of synaptic pathology in Alzheimer’s disease. Acta Neuropathol (Berl). 1991;81(4):428–433.
   Web of Science ®Google Scholar
• Sennvik K, Bogdanovic N, Volkmann I, Fastbom J, Benedikz E. Beta-secretase-cleaved amyloid precursor protein in Alzheimer brain: a morphologic study. J Cell Mol Med. 2004;8(1):127–134.
   Web of Science ®Google Scholar
• Henriques AG, Vieira SI, da Cruz E Silva EF, da Cruz E Silva OAB. Abeta promotes Alzheimer’s disease-like cytoskeleton abnormalities with consequences to APP processing in neurons. J Neurochem. 2010;113(3):761–771.
   Web of Science ®Google Scholar
• Chen JX, Yan SS. Role of mitochondrial amyloid-beta in Alzheimer’s disease. J Alzheimers Dis. 2010;20 Suppl 2:S569–S578.
   Google Scholar
• Kim C, Choi H, Jung ES, et al. HDAC6 inhibitor blocks amyloid beta-induced impairment of mitochondrial transport in hippocampal neurons. PloS One. 2012;7(8):e42983.
   PubMed Web of Science ®Google Scholar
• Hempen B, Brion JP. Reduction of acetylated alpha-tubulin immunoreactivity in neurofibrillary tangle-bearing neurons in Alzheimer’s disease. J Neuropathol Exp Neurol. 1996;55(9):964–972.
   Web of Science ®Google Scholar
• Cohen TJ, Guo JL, Hurtado DE, et al. The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat Commun. 2011;2:252.
   PubMed Web of Science ®Google Scholar
• Cook C, Carlomagno Y, Gendron TF, et al. Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance. Hum Mol Genet. 2014;23(1):104–116.
   PubMed Web of Science ®Google Scholar
• Noack M, Leyk J, Richter-Landsberg C. HDAC6 inhibition results in tau acetylation and modulates tau phosphorylation and degradation in oligodendrocytes. Glia. 2014;62(4):535–547.
   Web of Science ®Google Scholar
• Xiong Y, Zhao K, Wu J, Xu Z, Jin S, Zhang YQ. HDAC6 mutations rescue human tau-induced microtubule defects in Drosophila. Proc Natl Acad Sci U S A. 2013;110(12):4604–4609.
   PubMed Web of Science ®Google Scholar
• Govindarajan N, Rao P, Burkhardt S, et al. Reducing HDAC6 ameliorates cognitive deficits in a mouse model for Alzheimer’s disease. EMBO Mol Med. 2013;5(1):52–63.
   PubMed Web of Science ®Google Scholar
• Schiff PB, Horwitz SB. Taxol stabilizes microtubules in mouse fibroblast cells. Proc Natl Acad Sci U S A. 1980;77(3):1561–1565.
   PubMed Web of Science ®Google Scholar
• Shemesh OA, Spira ME. Rescue of neurons from undergoing hallmark tau-induced Alzheimer’s disease cell pathologies by the antimitotic drug paclitaxel. Neurobiol Dis. 2011;43(1):163–175.
   Web of Science ®Google Scholar
• Michaelis ML, Ranciat N, Chen Y, et al. Protection against beta-amyloid toxicity in primary neurons by paclitaxel (Taxol). J Neurochem. 1998;70(4):1623–1627.
   Web of Science ®Google Scholar
• Trojanowski JQ, Smith AB, Huryn D, Lee VM-Y. Microtubule-stabilising drugs for therapy of Alzheimer’s disease and other neurodegenerative disorders with axonal transport impairments. Expert Opin Pharmacother. 2005;6(5):683–686.
   PubMed Web of Science ®Google Scholar
• Brunden KR, Zhang B, Carroll J, et al. Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy. J Neurosci. 2010;30(41):13861–13866.
   PubMed Web of Science ®Google Scholar
• Zhang B, Carroll J, Trojanowski JQ, et al. The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice. J Neurosci. 2012;32(11):3601–3611.
   PubMed Web of Science ®Google Scholar
• Lee JJ, Swain SM. Peripheral neuropathy induced by microtubule-stabilizing agents. J Clin Oncol. 2006;24(10):1633–1642.
   PubMed Web of Science ®Google Scholar
• Bedard PL, Di Leo A, Piccart-Gebhart MJ. Taxanes: optimizing adjuvant chemotherapy for early-stage breast cancer. Nat Rev Clin Oncol. 2010;7(1):22–36.
   PubMed Web of Science ®Google Scholar
• Noh H, Seo H. Age-dependent effects of valproic acid in Alzheimer’s disease (AD) mice are associated with nerve growth factor (NGF) regulation. Neuroscience. 2014;266:255–265.
   PubMed Web of Science ®Google Scholar
• Qing H, He G, Ly PTT, et al. Valproic acid inhibits Abeta production, neuritic plaque formation, and behavioral deficits in Alzheimer’s disease mouse models. J Exp Med. 2008;205(12):2781–2789.
   PubMed Web of Science ®Google Scholar
• Ricobaraza A, Cuadrado-Tejedor M, Pérez-Mediavilla A, Frechilla D, Del Río J, García-Osta A. Phenylbutyrate ameliorates cognitive deficit and reduces tau pathology in an Alzheimer’s disease mouse model. Neuropsychopharmacol. 2009;34(7):1721–1732.
   PubMed Web of Science ®Google Scholar
• Zhang L, Liu C, Wu J, et al. Tubastatin A/ACY–1215 improves cognition in Alzheimer’s disease transgenic mice. J Alzheimers Dis. 2014; 41(4):1193–1205.
   PubMed Web of Science ®Google Scholar
• Wakabayashi K, Tanji K, Mori F, Takahashi H. The Lewy body in Parkinson’s disease: molecules implicated in the formation and degradation of alpha-synuclein aggregates. Neuropathol. 2007;27(5):494–506.
   PubMed Web of Science ®Google Scholar
• Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A, Yao TP. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell. 2003;115(6):727–738.
   PubMed Web of Science ®Google Scholar
• Donmez G, Outeiro TF. SIRT1 and SIRT2: emerging targets in neurodegeneration. EMBO Mol Med. 2013;5(3):344–352.
   PubMed Web of Science ®Google Scholar
• Fusco C, Micale L, Augello B, et al. HDAC6 mediates the acetylation of TRIM50. Cell Signal. 2014;26(2):363–369.
   Web of Science ®Google Scholar
• Yan J. Interplay between HDAC6 and its interacting partners: essential roles in the aggresome-autophagy pathway and neurodegenerative diseases. DNA Cell Biol. 2014;33(9):567–580.
   Web of Science ®Google Scholar
• Outeiro TF, Kontopoulos E, Altmann SM, et al. Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson’s disease. Science. 2007;317(5837):516–519.
   PubMed Web of Science ®Google Scholar
• Liu L, Arun A, Ellis L, Peritore C, Donmez G. SIRT2 enhances 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced nigrostriatal damage via apoptotic pathway. Front Aging Neurosci. 2014;6:184.
   PubMed Web of Science ®Google Scholar
• Bobrowska A, Paganetti P, Matthias P, Bates GP. Hdac6 knock-out increases tubulin acetylation but does not modify disease progression in the R6/2 mouse model of Huntington’s disease. PloS One. 2011;6(6):e20696.
   PubMed Web of Science ®Google Scholar
• Luthi-Carter R, Taylor DM, Pallos J, et al. SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis. Proc Natl Acad Sci U S A. 2010;107(17):7927–7932.
   PubMed Web of Science ®Google Scholar
• Ma Y, Chen H, He X, et al. NAD+ metabolism and NAD(+)-dependent enzymes: promising therapeutic targets for neurological diseases. Curr Drug Targets. 2012;13(2):222–229.
   Web of Science ®Google Scholar
• Bobrowska A, Donmez G, Weiss A, Guarente L, Bates G. SIRT2 ablation has no effect on tubulin acetylation in brain, cholesterol biosynthesis or the progression of Huntington’s disease phenotypes in vivo. PloS One. 2012;7(4):e34805.
   Web of Science ®Google Scholar
• Chopra V, Quinti L, Kim J, et al. The sirtuin 2 inhibitor AK-7 is neuroprotective in Huntington’s disease mouse models. Cell Rep. 2012; 2(6):1492–1497.
   PubMed Web of Science ®Google Scholar
• Suter U, Scherer SS. Disease mechanisms in inherited neuropathies. Nat Rev Neurosci. 2003;4(9):714–726.
   Web of Science ®Google Scholar
• Tanabe K, Takei K. Dynamic instability of microtubules requires dynamin 2 and is impaired in a Charcot-Marie-Tooth mutant. J Cell Biol. 2009;185(6):939–948.
   Web of Science ®Google Scholar
• D’ Ydewalle C, Krishnan J, Chiheb DM, et al. HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1-induced Charcot-Marie-Tooth disease. Nat Med. 2011;17(8):968–974.
   Web of Science ®Google Scholar
• Xu X, Kozikowski AP, Pozzo-Miller L. A selective histone deacetylase-6 inhibitor improves BDNF trafficking in hippocampal neurons from Mecp2 knockout mice: implications for Rett syndrome. Front Cell Neurosci. 2014;8:68.
   PubMed Web of Science ®Google Scholar
• Gold WA, Lacina TA, Cantrill LC, Christodoulou J. MeCP2 deficiency is associated with reduced levels of tubulin acetylation and can be restored using HDAC6 inhibitors. J Mol Med (Berl). Epub September 12, 2014.
   Google Scholar
• Piao Y-S, Wakabayashi K, Kakita A, et al. Neuropathology with clinical correlations of sporadic amyotrophic lateral sclerosis: 102 autopsy cases examined between 1962 and 2000. Brain Pathol. 2003;13(1):10–22.
   Web of Science ®Google Scholar
• Watanabe M, Dykes-Hoberg M, Culotta VC, Price DL, Wong PC, Rothstein JD. Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol Dis. 2001;8(6):933–941.
   PubMed Web of Science ®Google Scholar
• Pasinelli P, Brown RH. Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat Rev Neurosci. 2006;7(9):710–723.
   PubMed Web of Science ®Google Scholar
• Rosen DR, Siddique T, Patterson D, et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 1993;362(6415):59–62.
   PubMed Web of Science ®Google Scholar
• Chiu AY, Zhai P, Dal Canto MC, et al. Age-dependent penetrance of disease in a transgenic mouse model of familial amyotrophic lateral sclerosis. Mol Cell Neurosci. 1995;6(4):349–362.
   Web of Science ®Google Scholar
• Gurney ME, Pu H, Chiu AY, et al. Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Science. 1994;264(5166):1772–1775.
   PubMed Web of Science ®Google Scholar
• Boillée S, Vande Velde C, Cleveland DW. ALS: a disease of motor neurons and their nonneuronal neighbors. Neuron. 2006;52(1):39–59.
   PubMed Web of Science ®Google Scholar
• Yoo Y-E, Ko C-P. Treatment with trichostatin A initiated after disease onset delays disease progression and increases survival in a mouse model of amyotrophic lateral sclerosis. Exp Neurol. 2011;231(1):147–159.
   PubMed Web of Science ®Google Scholar
• Taes I, Timmers M, Hersmus N, et al. Hdac6 deletion delays disease progression in the SOD1G93A mouse model of ALS. Hum Mol Genet. 2013;22(9):1783–1790.
   PubMed Web of Science ®Google Scholar
• Gal J, Chen J, Barnett KR, Yang L, Brumley E, Zhu H. HDAC6 regulates mutant SOD1 aggregation through two SMIR motifs and tubulin acetylation. J Biol Chem. 2013;288(21):15035–15045.
   Web of Science ®Google Scholar
• Bruneteau G, Simonet T, Bauché S, et al. Muscle histone deacetylase 4 upregulation in amyotrophic lateral sclerosis: potential role in reinnervation ability and disease progression. Brain J Neurol. 2013;136(Pt 8):2359–2368.
   Google Scholar
• Rich DP, Anderson MP, Gregory RJ, et al. Expression of cystic fibrosis transmembrane conductance regulator corrects defective chloride channel regulation in cystic fibrosis airway epithelial cells. Nature. 1990;347(6291):358–363.
   PubMed Web of Science ®Google Scholar
• Ciofu O, Hansen CR, Høiby N. Respiratory bacterial infections in cystic fibrosis. Curr Opin Pulm Med. 2013;19(3):251–258.
   PubMed Web of Science ®Google Scholar
• Hodges CA, Grady BR, Mishra K, Cotton CU, Drumm ML. Cystic fibrosis growth retardation is not correlated with loss of Cftr in the intestinal epithelium. Am J Physiol Gastrointest Liver Physiol. 2011; 301(3):G528–G536.
   Web of Science ®Google Scholar
• Wright FA, Strug LJ, Doshi VK, et al. Genome-wide association and linkage identify modifier loci of lung disease severity in cystic fibrosis at 11p13 and 20q13.2. Nat Genet. 2011;43(6):539–546.
   PubMed Web of Science ®Google Scholar
• Emond MJ, Louie T, Emerson J, et al. Exome sequencing of extreme phenotypes identifies DCTN4 as a modifier of chronic Pseudomonas aeruginosa infection in cystic fibrosis. Nat Genet. 2012;44(8):886–889.
   Web of Science ®Google Scholar
• White NM, Jiang D, Burgess JD, Bederman IR, Previs SF, Kelley TJ. Altered cholesterol homeostasis in cultured and in vivo models of cystic fibrosis. Am J Physiol Lung Cell Mol Physiol. 2007;292(2):L476–L486.
   PubMed Web of Science ®Google Scholar
• Fredly H, Gjertsen BT, Bruserud O. Histone deacetylase inhibition in the treatment of acute myeloid leukemia: the effects of valproic acid on leukemic cells, and the clinical and experimental evidence for combining valproic acid with other antileukemic agents. Clin Epigenetics. 2013;5(1):12.
   PubMed Web of Science ®Google Scholar
• Lee Y-S, Lim K-H, Guo X, et al. The cytoplasmic deacetylase HDAC6 is required for efficient oncogenic tumorigenesis. Cancer Res. 2008;68(18):7561–7569.
   PubMed Web of Science ®Google Scholar
• Ketene AN, Roberts PC, Shea AA, Schmelz EM, Agah M. Actin filaments play a primary role for structural integrity and viscoelastic response in cells. Integr Biol Quant Biosci Nano Macro. 2012;4(5):540–549.
   Google Scholar
• Husain M, Cheung C-Y. Histone deacetylase 6 inhibits influenza A virus release by downregulating the trafficking of viral components to the plasma membrane via its substrate, acetylated microtubules. J Virol. 2014;88(19):11229–11239.
   PubMed Web of Science ®Google Scholar
• Husain M, Harrod KS. Enhanced acetylation of alpha-tubulin in influenza A virus infected epithelial cells. FEBS Lett. 2011;585(1):128–132.
   PubMed Web of Science ®Google Scholar
• Banerjee I, Miyake Y, Nobs SP, et al. Influenza A virus uses the aggresome processing machinery for host cell entry. Science. 2014; 346(6208):473–477.
   PubMed Web of Science ®Google Scholar
• Badding MA, Dean DA. Highly acetylated tubulin permits enhanced interactions with and trafficking of plasmids along microtubules. Gene Ther. 2013;20(6):616–624.
   PubMed Web of Science ®Google Scholar