HDAC6 as a potential therapeutic target for peripheral nerve disorders

References

• NINDS. Peripheral neuropathy fact sheet. NIH Pub. No. 15-4853. 2014.
   Google Scholar
• Tesfaye S, Boulton AJM, Dyck PJ, et al. Diabetic neuropathies: update on definitions, diagnostic criteria, estimation of severity, and treatments. Diabetes Care. 2010;2285–2293.
   PubMed Web of Science ®Google Scholar
• Karam C, Dyck PJB. Toxic neuropathies. Semin Neurol. 2015; 35(04): 448-457.
   Google Scholar
• England JD, Asbury AK. Peripheral neuropathy. Lancet. 2004;2151–2161.
   PubMedGoogle Scholar
• Baron R. Mechanisms of disease: neuropathic pain—a clinical perspective. Nat Clin Pract Neurol. 2006;2:95–106.
   PubMedGoogle Scholar
• Cashman CR, Höke A. Mechanisms of distal axonal degeneration in peripheral neuropathies. Neurosci Lett. 2015;596:33–50.
   PubMed Web of Science ®Google Scholar
• Grozinger CM, Hassig CA, Schreiber SL. Three proteins define a class of human histone deacetylases related to yeast Hda1p. Biochemistry. 1999;96:4868–4873.
   Google Scholar
• Cress WD, Seto E. Histone deacetylases, transcriptional control, and cancer. J Cell Physiol. 2000;184:1–16.
   PubMed Web of Science ®Google Scholar
• Zhang Y, Li N, Caron C, et al. HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. Embo J. 2003 Feb 28;22:1168–1179.
   PubMed Web of Science ®Google Scholar
• Kovacs JJ, Murphy PJ, Gaillard S, et al. HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Mol Cell. 2005 May 27;18:601–607.
   PubMed Web of Science ®Google Scholar
• Zhang X, Yuan Z, Zhang Y, et al. HDAC6 modulates cell motility by altering the acetylation level of cortactin. Mol Cell. 2007 July 24;27:197–213.
   PubMed Web of Science ®Google Scholar
• Ding G, Liu HD, Huang Q, et al. HDAC6 promotes hepatocellular carcinoma progression by inhibiting P53 transcriptional activity. FEBS Lett. 2013 Feb 14;587:880–886.
   PubMed Web of Science ®Google Scholar
• Kawaguchi Y, Kovacs JJ, McLaurin A, et al. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell. 2003 Dec 17;115:727–738.
   PubMed Web of Science ®Google Scholar
• Miyake Y, Keusch JJ, Wang L, et al. Structural insights into HDAC6 tubulin deacetylation and its selective inhibition. Nat Chem Biol. 2016;12:748–754.
   PubMed Web of Science ®Google Scholar
• Bertos NR, Gilquin B, Chan GKT, et al. Role of the tetradecapeptide repeat domain of human histone deacetylase 6 in cytoplasmic retention. J Biol Chem. 2004;279:48246–48254.
   PubMed Web of Science ®Google Scholar
• D’Ydewalle C, Bogaert E. Van den Bosch L. HDAC6 at the intersection of neuroprotection and neurodegeneration. Traffic. 2012 Mar 1;13:771–779.
   PubMed Web of Science ®Google Scholar
• Guo W, Naujock M, Fumagalli L, et al. HDAC6 inhibition reverses axonal transport defects in motor neurons derived from FUS-ALS patients. Nat Commun [Internet]. 2017;8:1–14.
   PubMed Web of Science ®Google Scholar
• Majid T, Griffin D, Criss Z, et al. Pharmocologic treatment with histone deacetylase 6 inhibitor (ACY-738) recovers Alzheimer’s disease phenotype in amyloid precursor protein/presenilin 1 (APP/PS1) mice. Alzheimer’s Dement Transl Res Clin Interv. 2015;1:170–181.
   PubMedGoogle Scholar
• Simões-Pires C, Zwick V, Nurisso A, et al. HDAC6 as a target for neurodegenerative diseases: what makes it different from the other HDACs? Mol Neurodegener. 2013;8:7.
   PubMed Web of Science ®Google Scholar
• Guedes-Dias P, de Proença J, Soares TR, et al. HDAC6 inhibition induces mitochondrial fusion, autophagic flux and reduces diffuse mutant huntingtin in striatal neurons. Biochim Biophys Acta Mol Basis Dis. 2015;1852:2484–2493.
   PubMed Web of Science ®Google Scholar
• Wang Z, Leng Y, Wang J, et al. Tubastatin A, an HDAC6 inhibitor, alleviates stroke-induced brain infarction and functional deficits: potential roles of α-tubulin acetylation and FGF-21 up-regulation. Sci Rep. 2016;6:1–12.
   PubMed Web of Science ®Google Scholar
• Van Helleputte L, Benoy V, Van den Bosch L. The role of histone deacetylase 6 (HDAC6) in neurodegeneration. 2014;5:1–13.
   Google Scholar
• Hirokawa N, Niwa S, Tanaka Y. Molecular motors in neurons: transport mechanisms and roles in brain function, development, and disease. Neuron [Internet]. 2010;68:610–638.
   PubMed Web of Science ®Google Scholar
• Griffin JW, Watson DF. Axonal transport in neurological disease. Ann Neurol. 1988;23:3–13.
   PubMed Web of Science ®Google Scholar
• Lloyd TE. Axonal transport disruption in peripheral nerve disease. J Peripher Nerv Syst. 2012;17:46–51.
   PubMedGoogle Scholar
• Zhao C, Takita J, Tanaka Y, et al. Charcot-Marie-Tooth disease type 2A caused by mutation in a microtubule motor KIF1Bbeta. Cell [Internet]. 2001;105:587–597. Available from: http://www.ncbi.nlm.nih.gov/pubmed/11389829
   PubMed Web of Science ®Google Scholar
• Weedon MN, Hastings R, Caswell R, et al. Exome sequencing identifies a DYNC1H1 mutation in a large pedigree with dominant Axonal Charcot-Marie-Tooth disease. Am J Hum Genet [Internet]. 2011;89:308–312.
   PubMed Web of Science ®Google Scholar
• Puls I, Jonnakuty C, LaMonte BH, et al. Mutant dynactin in motor neuron disease. Nat Genet. 2003;33:455–456.
   PubMed Web of Science ®Google Scholar
• LaMonte BH, Wallace KE, Holloway BA, et al. Disruption of dynein/dynactin inhibits axonal transport in motor neurons causing late-onset progressive degeneration. Neuron. 2002;34:715–727.
   PubMed Web of Science ®Google Scholar
• Langworthy MM, Appel B. Schwann cell myelination requires Dynein function. Neural Dev [Internet]. 2012;7:1–15. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3520773&tool=pmcentrez&rendertype=abstract
   PubMed Web of Science ®Google Scholar
• Brownlees J, Ackerley S, Grierson AJ, et al. Charcot-Marie-Tooth disease neurofilament mutations disrupt neurofilament assembly and axonal transport. Hum Mol Genet. 2002;11:2837–2844.
   PubMed Web of Science ®Google Scholar
• Yates DM, Manser C, De Vos KJ, et al. Neurofilament subunit (NFL) head domain phosphorylation regulates axonal transport of neurofilaments. Eur J Cell Biol. 2009;88:193–202.
   PubMed Web of Science ®Google Scholar
• Yoon BC, Jung H, Dwivedy A, et al. Local translation of extranuclear lamin B promotes axon maintenance. Cell [Internet]. 2012;148:752–764.
   PubMed Web of Science ®Google Scholar
• Sugimoto K, Yasujima M, Yagihashi S. Role of advanced glycation end products in diabetic neuropathy. Curr Pharm Des. 2008;14:953–961.
   PubMed Web of Science ®Google Scholar
• Prior R, Van Helleputte L, Benoy V, et al. Defective axonal transport: a common pathological mechanism in inherited and acquired peripheral neuropathies. Neurobiol Dis [ [Internet]. 2017;105:300–320.
   PubMed Web of Science ®Google Scholar
• Nicolini G, Monfrini M, Scuteri A. Axonal transport impairment in chemotherapy-induced peripheral neuropathy. Toxics. 2015;3:322–341.
   PubMed Web of Science ®Google Scholar
• Cavaletti G, Marmiroli P. Chemotherapy-induced peripheral neurotoxicity. Nat Rev Neurol. 2010;12:657–667.
   Google Scholar
• Höke A. Mechanisms of Disease: what factors limit the success of peripheral nerve regeneration in humans? Nat Clin Pract Neurol. 2006;2:448–454.
   PubMedGoogle Scholar
• Chakraborti S, Natarajan K, Curiel J, et al. The emerging role of the tubulin code: from the tubulin molecule to neuronal function and disease. Cytoskeleton. 2016;73:521–550.
   PubMed Web of Science ®Google Scholar
• Janke C, Chloë bulinski J. Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions. Nat Rev Mol Cell Biol. 2011;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;27:3571–3583.
   PubMed Web of Science ®Google Scholar
• Rogowski K, van Dijk J, Magiera MM, et al. A family of protein-deglutamylating enzymes associated with neurodegeneration. Cell. 2010;143:564–578.
   PubMed Web of Science ®Google Scholar
• De Vos KJ, Hafezparast M. Neurobiology of axonal transport defects in motor neuron diseases: opportunities for translational research? Neurobiol Dis. 2017;105:283–299.
   PubMed Web of Science ®Google Scholar
• Hubbert C, Guardiola A, Shao R, et al. HDAC6 is a microtubule-associated deacetylase. Nature. 2002 May 25;417:455–458.
   PubMed Web of Science ®Google Scholar
• Matsuyama A, Shimazu T, Sumida Y, et al. In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation. Embo J. 2002 Dec 18;21:6820–6831.
   PubMed Web of Science ®Google Scholar
• Zilberman Y, Ballestrem C, Carramusa L, et al. Regulation of microtubule dynamics by inhibition of the tubulin deacetylase HDAC6. J Cell Sci. 2009 Sep 10;122:3531–3541.
   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 Nov 7;16:2166–2172.
   PubMed Web of Science ®Google Scholar
• Chen S, Owens GC, Makarenkova H, et al. HDAC6 regulates mitochondrial transport in hippocampal neurons. PLoS One. 2010 Jun 4;5:e10848.
   PubMed Web of Science ®Google Scholar
• Cai Q, Sheng ZH. Moving or stopping mitochondria: miro as a traffic cop by sensing calcium. Neuron. 2009;61:493–496.
   PubMed Web of Science ®Google Scholar
• Wang X, Schwarz TL. The mechanism of Ca2+-dependent regulation of kinesin-mediated mitochondrial motility. Cell [Internet]. 2009;136:163–174.
   PubMed 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 [Internet]. 2011;17:968–974.
   PubMed Web of Science ®Google Scholar
• Benoy V, Van Helleputte L, Prior R, et al. HDAC6 is a therapeutic target in mutant GARS-induced Charcot-Marie-Tooth disease. Brain [Internet]. 2018;1–15. Available from. http://www.ncbi.nlm.nih.gov/pubmed/29415205%0Ahttps://academic.oup.com/brain/advance-article/doi/10.1093/brain/awx375/4838963 :
   PubMed Web of Science ®Google Scholar
• Van Helleputte L, Kater M, Cook DP, et al. Inhibition of histone deacetylase 6 (HDAC6) protects against vincristine-induced peripheral neuropathies and inhibits tumor growth. Neurobiol Dis [ [Internet]. 2018;111:59–69.
   PubMed Web of Science ®Google Scholar
• Krukowski K, Ma J, Golonzhka O, et al. HDAC6 inhibition effectively reverses chemotherapy-induced peripheral neuropathy. Pain. 2017;158:1126–1137.
   PubMed Web of Science ®Google Scholar
• Mo Z, Zhao X, Liu H, et al. Aberrant GlyRS-HDAC6 interaction linked to axonal transport deficits in Charcot-Marie-Tooth neuropathy. Nat Commun. 2018;9:1007.
   PubMed Web of Science ®Google Scholar
• Jung J, Cai W, Lee HK, et al. Actin polymerization is essential for myelin sheath fragmentation during Wallerian degeneration. J Neurosci. 2011;31:2009–2015.
   PubMed Web of Science ®Google Scholar
• Bacon C, Lakics V, Machesky L, et al. N-WASP regulates extension of filopodia and processesby oligodendrocyte progenitors, oligodendrocytes, andschwann cells—implications for axon ensheathmentat myelination. Glia. 2007;55:844–858.
   PubMed Web of Science ®Google Scholar
• FernandezValle C, Gorman D, Gomez AM, et al. Actin plays a role in both changes in cell shape and gene- expression associated with Schwann cell myelination. J Neurosci. 1997;17:241–250.
   PubMed Web of Science ®Google Scholar
• Goldberg AL. Protein degradation and protection against misfolded or damaged proteins. Nature. 2003 Dec 20;426:895–899.
   PubMed Web of Science ®Google Scholar
• Thibaudeau TA, Anderson RT, Smith DM. A common mechanism of proteasome impairment by neurodegenerative disease-associated oligomers. Nat Commun. 2018.
   PubMed Web of Science ®Google Scholar
• Dantuma NP, Bott LC. The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution. Front Mol Neurosci. 2014;7.
   PubMed Web of Science ®Google Scholar
• Cuervo AM, Wong E. Chaperone-mediated autophagy: roles in disease and aging. Cell Res. 2014;24:92–104.
   PubMed Web of Science ®Google Scholar
• Züchner S, Vance JM. Molecular genetics of autosomal-dominant axonal charcot-marie-tooth disease. NeuroMolecular Med. 2006;8:63–74.
   PubMed Web of Science ®Google Scholar
• Lee SM, Chin LS, Li L. Protein misfolding and clearance in demyelinating peripheral neuropathies: therapeutic implications. Commun Integr Biol. 2012 Apr 7;5:107–110.
   PubMedGoogle Scholar
• Piperi C, Adamopoulos C, Dalagiorgou G, et al. Crosstalk between advanced glycation and endoplasmic reticulum stress: emerging therapeutic targeting for metabolic diseases. J Clin Endocrinol Metab. 2012;97:2231–2242.
   PubMed Web of Science ®Google Scholar
• Cameron NE. Role of endoplasmic reticulum stress in diabetic neuropathy. Diabetes. 2013;62:696–697.
   Web of Science ®Google Scholar
• Lupachyk S, Watcho P, Stavniichuk R, et al. Endoplasmic reticulum stress plays a key role in the pathogenesis of diabetic peripheral neuropathy. Diabetes. 2013;62:944–952.
   PubMed Web of Science ®Google Scholar
• Queisser MA, Yao D, Geisler S, et al. Hyperglycemia impairs proteasome function by methylglyoxal. Diabetes. 2010;59:670–678.
   PubMed Web of Science ®Google Scholar
• Henstridge DC, Whitham M, Febbraio MA. Chaperoning to the metabolic party: the emerging therapeutic role of heat-shock proteins in obesity and type 2 diabetes. Mol Metab. 2014;3:781–793.
   PubMed Web of Science ®Google Scholar
• Meregalli C. An Overview of Bortezomib-Induced Neurotoxicity. Toxics. 2015;3:294–303.
   PubMed Web of Science ®Google Scholar
• Elder RM, Jayaraman A. Sequence-specific recognition of cancer drug-DNA adducts by HMGB1a repair protein. Biophys J. 2012;102:2331–2338.
   PubMed Web of Science ®Google Scholar
• LaPointe NE, Morfini G, Brady ST, et al. Effects of eribulin, vincristine, paclitaxel and ixabepilone on fast axonal transport and kinesin-1 driven microtubule gliding: implications for chemotherapy-induced peripheral neuropathy. Neurotoxicology. 2013 May 29;37:231–239.
   PubMed Web of Science ®Google Scholar
• Massey AC, Zhang C, Cuervo AM. Chaperone-mediated autophagy in aging and disease. Curr Top Dev Biol. 2006 Jun 20;73:205–235.
   PubMed Web of Science ®Google Scholar
• Haidar M, Timmerman V. Autophagy as an emerging common pathomechanism in inherited peripheral neuropathies. Front Mol Neurosci. 2017;10:1–17.
   PubMed Web of Science ®Google Scholar
• Boyault C, Sadoul K, Pabion M, et al. HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination. Oncogene. 2007;26:5468–5476.
   PubMed Web of Science ®Google Scholar
• Richter-Landsberg C The α-tubulin deacetylase HDAC6 in aggresome formation and autophagy: implications for neurodegeneration. In: Autophagy cancer, other pathol. Inflammation, immunity, infect. Aging. Hayat MA, editor. Academic Press; 2015;5:273–282.
   Google Scholar
• Boyault C, Gilquin B, Zhang Y, et al. HDAC6-p97/VCP controlled polyubiquitin chain turnover. Embo J. 2006 Jul 1;25:3357–3366.
   PubMed Web of Science ®Google Scholar
• Johnson JO, Mandrioli J, Benatar M, et al. Exome sequencing reveals VCP mutations as a cause of familial ALS. Neuron. 2010;68:857–864.
   PubMed Web of Science ®Google Scholar
• Seigneurin-Berny D, Verdel A, Curtet S, et al. Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways. Mol Cell Biol. 2001 Nov 2;21:8035–8044.
   PubMed Web of Science ®Google Scholar
• Kopito RR. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 2000 Dec 21;10:524–530.
   PubMed Web of Science ®Google Scholar
• Waza M, Adachi H, Katsuno M, et al. Modulation of Hsp90 function in neurodegenerative disorders: a molecular-targeted therapy against disease-causing protein. J Mol Med. 2006 Jul 3;84:635–646.
   PubMed Web of Science ®Google Scholar
• Boyault C, Zhang Y, Fritah S, et al. HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregates. Genes Dev. 2007 Sep 6;21:2172–2181.
   PubMed Web of Science ®Google Scholar
• Pandey UB, Nie Z, Batlevi Y, et al. HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature. 2007 Jun 15;447:859–863.
   PubMed Web of Science ®Google Scholar
• Levine B, Klionsky DJ. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev Cell. 2004 Apr 8;6:463–477.
   PubMed Web of Science ®Google Scholar
• Lee JY, Koga H, Kawaguchi Y, et al. HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy. Embo J. 2010 Jan 16;29:969–980.
   PubMed Web of Science ®Google Scholar
• Liebl D, Griffiths G. Transient assembly of F-actin by phagosomes delays phagosome fusion with lysosomes in cargo-overloaded macrophages. J Cell Sci. 2009 Jul 30;122:2935–2945.
   PubMed Web of Science ®Google Scholar
• Iwata A, Riley BE, Johnston JA, et al. HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem. 2005 Sep 30;280:40282–40292.
   PubMed Web of Science ®Google Scholar
• Anderson P, Kedersha N. RNA granules. J Cell Biol. 2006 Mar 8;172:803–808.
   PubMed Web of Science ®Google Scholar
• Mazroui R, Di marco S, Kaufman RJ, et al. Inhibition of the ubiquitin-proteasome system induces stress granule formation. Mol Biol Cell. 2007 May 4;18:2603–2618.
   PubMed Web of Science ®Google Scholar
• Kwon S, Zhang Y, Matthias P. The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response. Genes Dev. 2007 Dec 15;21:3381–3394.
   PubMed Web of Science ®Google Scholar
• Kappeler KV, Zhang J, Dinh TN, et al. Histone deacetylase 6 associates with ribosomes and regulates de novo protein translation during arsenite stress. Toxicol Sci. 2012;127:246–255.
   PubMed Web of Science ®Google Scholar
• van Paassen BW, van der Kooi AJ, van Spaendonck-Zwarts KY, et al. PMP22 related neuropathies: charcot-marie-tooth disease type 1A and hereditary neuropathy with liability to pressure palsies. Orphanet J Rare Dis [Internet]. 2014;9:38. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3994927&tool=pmcentrez&rendertype=abstract
   PubMed Web of Science ®Google Scholar
• Shy ME, Jáni A, Krajewski K, et al. Phenotypic clustering in MPZ mutations. Brain. 2004;127:371–384.
   PubMed Web of Science ®Google Scholar
• Sevilla T, Sivera R, Martínez-Rubio D, et al. The EGR2 gene is involved in axonal Charcot-Marie-Tooth disease. Eur J Neurol. 2015;22:1548–1555.
   PubMed Web of Science ®Google Scholar
• Nagarajan R, Svaren J, Le N, et al. EGR2 mutations in inherited neuropathies dominant-negatively inhibit myelin gene expression. Neuron. 2001;30:355–368.
   PubMed Web of Science ®Google Scholar
• LeBlanc SE, Ward RM, Svaren J. Neuropathy-associated Egr2 mutants disrupt cooperative activation of myelin protein zero by Egr2 and Sox10. Mol Cell Biol. 2007;27:3521–3529.
   PubMed Web of Science ®Google Scholar
• Clemence A, Mirsky R, Jessen KR. Non-myelin-forming Schwann cells proliferate rapidly during Wallerian degeneration in the rat sciatic nerve. J Neurocytol. 1989;18:185–192.
   PubMedGoogle Scholar
• Jessen KR, Mirsky R. The repair Schwann cell and its function in regenerating nerves. J Physiol. 2016;594:3521–3531.
   PubMed Web of Science ®Google Scholar
• Arthur-Farraj PJ, Latouche M, Wilton DK, et al. c-Jun reprograms schwann cells of injured nerves to generate a repair cell essential for regeneration. Neuron. 2012;75:633–647.
   PubMed Web of Science ®Google Scholar
• de Waegh S, Brady ST. Altered slow axonal transport and regeneration in a, myelin- deficient mutant mouse : the trembler as an in viva model for schwann cell-axon interactions. J Neurosci. 1990;10:1855–1865.
   PubMed Web of Science ®Google Scholar
• de Waegh S, Lee V, Brady S. Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating schwann cells. Cell. 1992;68:451–463.
   PubMed Web of Science ®Google Scholar
• Vavlitou N, Sargiannidou I, Markoullis K, et al. Axonal pathology precedes demyelination in a mouse model of x-linked demyelinating/type i charcot-marie tooth (CMT1X) neuropathy. J Neuropathol Exp Neurol. 2011;69:945–958.
   Web of Science ®Google Scholar
• Brügger V, Duman M, Bochud M, et al. Delaying histone deacetylase response to injury accelerates conversion into repair Schwann cells and nerve regeneration. Nat Commun. 2017;14272:1–16.
   Google Scholar
• He X, Zhang L, Queme LF, et al. A histone deacetylase 3–dependent pathway delimits peripheral myelin growth and functional regeneration. Nat Med [Internet]. 2018;24:338–351. doi:10.1038/nm.4483.
   PubMed Web of Science ®Google Scholar
• Hung H, Kohnken R, Svaren J. The nucleosome remodeling and deacetylase chromatin remodeling (NuRD) complex is required for peripheral nerve myelination. J Neurosci [Internet]. 2012;32:1517–1527. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3292862&tool=pmcentrez&rendertype=abstract
   PubMed Web of Science ®Google Scholar
• Mager GM, Ward RM, Srinivasan R, et al. Active gene repression by the Egr2·NAB complex during peripheral nerve myelination. J Biol Chem. 2008;283:18187–18197.
   PubMed Web of Science ®Google Scholar
• Xue YT, Wong JM, Moreno GT, et al. NURD, a novel complex with both ATP-dependent chromatin- remodeling and histone deacetylase activities. Mol Cell. 1998;2:851–861.
   PubMed Web of Science ®Google Scholar
• Noritsugu K, Ito A, Nakao Y, et al. Identification of zinc finger transcription factor EGR2 as a novel acetylated protein. Biochem Biophys Res Commun. 2017;489:455–459.
   PubMed Web of Science ®Google Scholar
• Akimova T, Beier UH, Liu Y, et al. Histone/protein deacetylases and T-cell immune responses. Blood. 2012;119:2443–2451.
   PubMed Web of Science ®Google Scholar
• Cheng F, Lienlaf M, Wang H-W, et al. A novel role for histone deacetylase 6 in the regulation of the tolerogenic STAT3/IL-10 pathway in APCs. J Immunol [Internet]. 2014;193:2850–2862. doi:10.4049/jimmunol.1302778.
   PubMed Web of Science ®Google Scholar
• Xu C, Bailly-Maitre B, Reed JC. Endoplasmic reticulum stress: cell life and death decisions. J Clin Invest. 2005;115:2656–2664.
   PubMed Web of Science ®Google Scholar
• Viader A, Sasaki Y, Kim S, et al. Aberrant schwann cell lipid metabolism linked to mitochondrial deficits leads to axon degeneration and neuropathy. Neuron. 2013;77:886–898.
   PubMed Web of Science ®Google Scholar
• Lin MT, Beal MF. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature. 2006 Oct 20;443:787–795.
   PubMed Web of Science ®Google Scholar
• Podratz JL, Lee H, Knorr P, et al. Cisplatin induces mitochondrial deficits in Drosophila larval segmental nerve. Neurobiol Dis. 2017;97:60–69.
   PubMed Web of Science ®Google Scholar
• Dalakas MC, Semino-Mora C, Leon-Monzon M. Mitochondrial alterations with mitochondrial DNA depletion in the nerves of AIDS patients with peripheral neuropathy induced by 2′3′-dideoxycytidine (DDC). Lab Investig. 2001;81:1537–1544.
   PubMed Web of Science ®Google Scholar
• Fernyhough P, Roy Chowdhury SK, Schmidt RE. Mitochondrial stress and the pathogenesis of diabetic neuropathy. Expert Rev Endocrinol Metab. 2010;5:39–49.
   PubMedGoogle Scholar
• Niemann A, Berger P, Suter U. Pathomechanisms of mutant proteins in Charcot-Marie-Tooth Disease. Neuromolecular Med. 2006;8:217–241.
   PubMed Web of Science ®Google Scholar
• Saporta MA, Dang V, Volfson D, et al. Axonal Charcot-Marie-Tooth disease patient-derived motor neurons demonstrate disease-specific phenotypes including abnormal electrophysiological properties. Exp Neurol [Internet]. 2015;263:190–199.
   PubMed Web of Science ®Google Scholar
• Misko A, Jiang S, Wegorzewska I, et al. Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex. J Neurosci [Internet]. 2010;30:4232–4240. Available from: http://www.ncbi.nlm.nih.gov/pubmed/20335458%5Cnhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2852190/pdf/nihms189508.pdf
   PubMed Web of Science ®Google Scholar
• Baloh RH, Schmidt RE, Pestronk A, et al. Altered axonal mitochondrial transport in the pathogenesis of Charcot-Marie-Tooth disease from mitofusin 2 mutations. J Neurosci [Internet]. 2007;27:422–430. Available from: http://www.ncbi.nlm.nih.gov/pubmed/17215403
   PubMed Web of Science ®Google Scholar
• Wood ZA, Schroder E, Robin Harris J, et al. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem Sci. 2003 Jan 9;28:32–40.
   PubMed Web of Science ®Google Scholar
• Moon JC, Kim GM, Kim EK, et al. Reversal of 2-Cys peroxiredoxin oligomerization by sulfiredoxin. Biochem Biophys Res Commun. 2013 Feb 12;432:291–295.
   PubMed Web of Science ®Google Scholar
• Parmigiani RB, Xu WS, Venta-Perez G, et al. HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation. Proc Natl Acad Sci U S A. 2008 Jul 9;105:9633–9638.
   PubMed Web of Science ®Google Scholar
• Choi H, Kim HJ, Kim J, et al. Increased acetylation of Peroxiredoxin1 by HDAC6 inhibition leads to recovery of Aβ-induced impaired axonal transport. Mol Neurodegener. 2017;12:1–14.
   PubMed Web of Science ®Google Scholar
• Stys PK, Sontheimer H, Ransom BR, et al. Noninactivating, tetrodotoxin-sensitive Na+ conductance in rat optic nerve axons. Proc Natl Acad Sci USA [Internet]. 1993;90:6976–6980. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=47058&tool=pmcentrez&rendertype=abstract
   PubMed Web of Science ®Google Scholar
• Stys PK, Waxman SG, Ransom BR. Ionic mechanisms of anoxic injury in mammalian CNS white matter: role of Na+ channels and Na(+)-Ca2+ exchanger. J Neurosci [Internet]. 1992;12:430–439. Available from: http://www.jneurosci.org/content/12/2/430.abstract
   PubMed Web of Science ®Google Scholar
• Landouré G, Zdebik AA, Martinez TL, et al. Mutations in TRPV4 cause Charcot-Marie-Tooth disease type 2C. Nat Genet [ [Internet]. 2009;42:170–174. doi:10.1038/ng.512.
   PubMed Web of Science ®Google Scholar
• Auer-Grumbach M, Olschewski A, Papić L, et al. Alterations in the ankyrin domain of TRPV4 cause congenital distal SMA, scapuloperoneal SMA and HMSN2C. Nat Genet [ [Internet]. 2010;42:160–164. doi:10.1038/ng.508.
   PubMed Web of Science ®Google Scholar
• Kann O, Kovacs R. Mitochondria and neuronal activity. AJP Cell Physiol. 2006;292:C641–C657.
   Google Scholar
• Jaggi AS, Singh N. Mechanisms in cancer-chemotherapeutic drugs-induced peripheral neuropathy. Toxicology. 2012;291:1–9.
   PubMed Web of Science ®Google Scholar
• Kumar P, Kumar D, Jha SK, et al. Ion channels in neurological disorders. Adv Protein Chem Struct Biol Elsevier Ltd. 2016;103:97–136.
   Google Scholar
• Aromolaran KA, Goldstein PA. Ion channels and neuronal hyperexcitability in chemotherapy-induced peripheral neuropathy. Mol Pain. 2017;13.
   PubMed Web of Science ®Google Scholar
• Hofmeijer J, Franssen H, van Schelven LJ, et al. Why are sensory axons more vulnerable for ischemia than motor axons? PLoS One. 2013;8.
   PubMed Web of Science ®Google Scholar
• Brockington A, Ning K, Heath PR, et al. Unravelling the enigma of selective vulnerability in neurodegeneration: motor neurons resistant to degeneration in ALS show distinct gene expression characteristics and decreased susceptibility to excitotoxicity. Acta Neuropathol. 2013;125:95–109.
   PubMed Web of Science ®Google Scholar
• Spence S, Deurinck M, Ju H, et al. Histone deacetylase inhibitors prolong cardiac repolarization through transcriptional mechanisms. Toxicol Sci. 2016;153:39–54.
   PubMed Web of Science ®Google Scholar
• Zhang D, Wu CT, Qi XY, et al. Activation of Histone Deacetylase-6 (HDAC6) induces contractile dysfunction through derailment of alpha-tubulin proteostasis in experimental and human atrial fibrillation. Circulation [Internet]. 2013;6. Available from: http://www.ncbi.nlm.nih.gov/pubmed/24146251
   Google Scholar
• Kempuraj D, Thangavel R, Selvakumar GP, et al. Brain and peripheral atypical inflammatory mediators potentiate neuroinflammation and neurodegeneration. Front Cell Neurosci. 2017;11.
   PubMed Web of Science ®Google Scholar
• Vlassara H, Brownlee M, Cerami A. High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules. Proc Natl Acad Sci U S A. 1985;82:5588–5592.
   PubMed Web of Science ®Google Scholar
• Yeh CH, Sturgis L, Haidacher J, et al. Requirement for p38 and p44/p42 mitogen-activated protein kinases in RAGE-mediated nuclear factor-kappaB transcriptional activation and cytokine secretion. Diabetes. 2001;50:1495–1504.
   PubMed Web of Science ®Google Scholar
• Zhu J, Coyne CB, Sarkar SN. PKC alpha regulates Sendai virus-mediated interferon induction through HDAC6 and ? 2-catenin. Embo J. 2011;30:4838–4849.
   PubMed Web of Science ®Google Scholar
• Yang C-J, Liu Y-P, Dai H-Y, et al. Nuclear HDAC6 inhibits invasion by suppressing NF-kB/MMP2 and is inversely correlated with metastasis of non-small cell lung cancer. Oncotarget [Internet]. 2015;6:30263–30276. Available from: http://www.oncotarget.com/fulltext/4749
   PubMedGoogle Scholar
• Powers JJ, Maharaj KK, Sahakian E, et al. Histone Deacetylase 6 (HDAC6) as a regulator of immune Check-Point Molecules in Chronic Lymphocytic Leukemia (CLL). Blood. 2014;124:3311.
   Web of Science ®Google Scholar
• Hance KW, Anderson WF, Devesa SS, et al. Trends in inflammatory breast carcinoma incidence and survival: the surveillance, epidemiology, and end results program at the national cancer institute. JNCI J Natl Cancer Inst. 2005;97:966–975.
   Web of Science ®Google Scholar
• Santo L, Hideshima T, Kung AL, et al. Preclinical activity, pharmacodynamic, and pharmacokinetic properties of a selective HDAC6 inhibitor, ACY-1215, in combination with bortezomib in multiple myeloma. Blood. 2012;119:2579–2589.
   PubMed Web of Science ®Google Scholar
• Vogl DT, Raje NS, Jagannath S, et al. Ricolinostat (ACY-1215), the first selective HDAC6 inhibitor, in combination with bortezomib and dexamethasone in patients with relapsed or relapsed-and-refractory multiple myeloma: phase 1b results (ACY-100 Study). Blood. 2015;126:1827.
   Web of Science ®Google Scholar
• de Zoeten EF, Wang L, Butler K, et al. Histone deacetylase 6 and heat shock protein 90 control the functions of Foxp3(+) T-regulatory cells. Mol Cell Biol. 2011;31:2066–2078.
   PubMed Web of Science ®Google Scholar
• Shakespear MR, Halili MA, Irvine KM, et al. Histone deacetylases as regulators of inflammation and immunity. Trends Immunol. 2011;32:335–343.
   PubMed Web of Science ®Google Scholar
• Seidel C, Schnekenburger M, Dicato M, et al. Histone deacetylase 6 in health and disease. Epigenomics. 2015;7:103–118.
   PubMed Web of Science ®Google Scholar
• Saifi GM, Szigeti K, Snipes GJ, et al. Molecular mechanisms, diagnosis, and rational approaches to management of and therapy for Charcot-Marie-Tooth disease and related peripheral neuropathies. J Investig Med. 2003;51:261–283.
   PubMed Web of Science ®Google Scholar
• Feldman EL. Oxidative stress and diabetic neuropathy: a new understanding of an old problem. J Clin Invest. 2003;111(4):431–433.
   PubMed Web of Science ®Google Scholar
• Areti A, Yerra VG, Naidu V, et al. Oxidative stress and nerve damage: role in chemotherapy induced peripheral neuropathy. Redox Biol. 2014;2:289–295.
   PubMed Web of Science ®Google Scholar
• Albano E. Alcohol, oxidative stress and free radical damage. Proc Nutr Soc. 2006;65:278–290.
   PubMed Web of Science ®Google Scholar
• Mccall KA, Huang -C-C, Fierke CA. Zinc and health: current status and future directions function and mechanism of zinc metalloenzymes 1. J Nutr. 2000;130:1437–1446.
   PubMed Web of Science ®Google Scholar
• Krämer OH, Mahboobi S, Sellmer A. Drugging the HDAC6-HSP90 interplay in malignant cells. Trends Pharmacol Sci. 2014;35:501–509.
   PubMed Web of Science ®Google Scholar
• Tang G, Wong JC, Zhang W, et al. Identification of a novel aminotetralin class of HDAC6 and HDAC8 selective inhibitors. J Med Chem. 2014;57:8026–8034.
   PubMed Web of Science ®Google Scholar
• Bergman JA, Woan K, Perez-Villarroel P, et al. Selective histone deacetylase 6 inhibitors bearing substituted urea linkers inhibit melanoma cell growth. J Med Chem. 2012;55:9891–9899.
   PubMed Web of Science ®Google Scholar
• Kuendgen A, Schmid M, Schlenk R, et al. The histone deacetylase (HDAC) inhibitor valproic acid as monotherapy or in combination with all-trans retinoic acid in patients with acute myeloid leukemia. Cancer. 2006;106:112–119.
   PubMed Web of Science ®Google Scholar
• Pal D, Saha S. Hydroxamic acid - A novel molecule for anticancer therapy. J Adv Pharm Technol Res [Internet]. 2012;3:92. Available from: http://www.japtr.org/text.asp?2012/3/2/92/97281
   PubMedGoogle Scholar
• Chateauvieux S, Morceau F, Dicato M, et al. Molecular and therapeutic potential and toxicity of valproic acid. J Biomed Biotechnol [Internet];2010:479364. Available from: http://www.hindawi.com/journals/bmri/2010/479364/
   PubMedGoogle Scholar
• Ghodke-Puranik Y, Thorn CF, Lamba JK, et al. Valproic acid pathway: pharmacokinetics and pharmacodynamics. Pharmacogenet Genomics. 2013;23:236–241.
   PubMed Web of Science ®Google Scholar
• Ueda H, Nakajima H, Hori Y, et al. FR901228, A novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum no 968.1. Taxonomy, fermentation, isolation, physicochemical and biological properties and antitumor activity. J Antibiot (Tokyo). 1994;47:301–310
   PubMed Web of Science ®Google Scholar
• HIGHLIGHTS OF PRESCRIBING INFORMATION FOR ISTODAX® (romidepsin) [Internet]. 2016. Available from: ISTBAXPI.007/PPI.007 7/2016.
   Google Scholar
• Subramanian S, Bates SE, Wright JJ, et al. Clinical toxicities of histone deacetylase inhibitors. Pharmaceuticals. 2010;3:2751–2767.
   Google Scholar
• Xu S, De Veirman K, Vanderkerken K, et al. Vorinostat-induced bone loss might be related to drug toxicity. Bone [Internet]. 2013;57:384–385.
   PubMed Web of Science ®Google Scholar
• Doi T, Hamaguchi T, Shirao K, et al. Evaluation of safety, pharmacokinetics, and efficacy of vorinostat, a histone deacetylase inhibitor, in the treatment of gastrointestinal (GI) cancer in a phase i clinical trial. Int J Clin Oncol. 2013;18:87–95.
   PubMed Web of Science ®Google Scholar
• Hamberg P, Woo MM, Chen LC, et al. Effect of ketoconazole-mediated CYP3A4 inhibition on clinical pharmacokinetics of panobinostat (LBH589), an orally active histone deacetylase inhibitor. Cancer Chemother Pharmacol. 2011;68:805–813.
   PubMed Web of Science ®Google Scholar
• Warren KE, McCully C, Dvinge H, et al. Plasma and cerebrospinal fluid pharmacokinetics of the histone deacetylase inhibitor, belinostat (PXD101), in non-human primates. Cancer Chemother Pharmacol. 2008;62:433–437.
   PubMed Web of Science ®Google Scholar
• Witt O, Deubzer HE, Milde T, et al. HDAC family: what are the cancer relevant targets? Cancer Lett [ [Internet]. 2009;277:8–21.
   PubMed Web of Science ®Google Scholar
• Su H, Altucci L, You Q. Competitive or noncompetitive, that’s the question: research toward histone deacetylase inhibitors. Mol Cancer Ther [Internet]. 2008;7:1007–1012. doi:10.1158/1535-7163.MCT-07-2289.
   PubMed Web of Science ®Google Scholar
• Li Y, Shin D, Kwon SH. Histone deacetylase 6 plays a role as a distinct regulator of diverse cellular processes. FEBS J. 2013;280:775–793.
   PubMed Web of Science ®Google Scholar
• Hai Y, Christianson DW. Histone deacetylase 6 structure and molecular basis of catalysis and inhibition. Nat Chem Biol. 2016;741–747.
   PubMed Web of Science ®Google Scholar
• Goracci L, Deschamps N, Randazzo GM, et al. A rational approach for the identification of non-hydroxamate HDAC6-selective inhibitors. Sci Rep [ [Internet]. 2016;6:1–12.
   PubMed Web of Science ®Google Scholar
• Haggarty SJ, Koeller KM, Wong JC, et al. Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc Natl Acad Sci [Internet]. 2003;100:4389–4394. doi:10.1073/pnas.0430973100.
   PubMed Web of Science ®Google Scholar
• Dallavalle S, Pisano C, Zunino F. Development and therapeutic impact of HDAC6-selective inhibitors. Biochem Pharmacol [Internet]. 2012;84:756–765.
   PubMed Web of Science ®Google Scholar
• Kalin JH, Bergman JA. Development and therapeutic implications of selective histone deacetylase 6 inhibitors. J Med Chem. 2013;56:6297–6313.
   PubMed Web of Science ®Google Scholar
• Porter NJ, Mahendran A, Breslow R, et al. Unusual zinc-binding mode of HDAC6-selective hydroxamate inhibitors. Proc Natl Acad Sci [Internet]. 2017;114:201718823. doi:10.1073/pnas.1718823114.
   Web of Science ®Google Scholar
• Porter NJ, Osko JD, Diedrich D, et al. Histone Deacetylase 6-selective inhibitors and the influence of capping groups on hydroxamate-zinc denticity. J Med Chem [Internet]. 2018;61: acs.jmedchem.8b01013. doi:10.1021/acs.jmedchem.8b01013.
   Google Scholar
• Groutas WC, Giri PK, Crowley JP, et al. The lossen rearrangement in biological systems. Inactivation of leukocyte elastase and alpha-chymotrypsin by (DL)-3-benzyl-N- (methanesulfonyloxy) succinimide. Biochem Biophys Res Commun. 1986;141:741–748.
   PubMed Web of Science ®Google Scholar
• Lee MS, Isobe M. Metabolic activation of the potent mutagen, 2-naphthohydroxamic acid, in salmonella typhimurium TA98. Cancer Res. 1990;50:4300–4307.
   PubMed Web of Science ®Google Scholar
• Shen S, Kozikowski AP. Why hydroxamates may not be the best histone deacetylase inhibitors - what some may have forgotten or would rather forget? ChemMedChem. 2016;11:15–21.
   PubMed Web of Science ®Google Scholar
• Simões-Pires CA, Bertrand P, Cuendet M. Novel histone deacetylase 6 (HDAC6) selective inhibitors: a patent evaluation (WO2014181137). Expert Opin Ther Pat. 2017;229–236.
   PubMed Web of Science ®Google Scholar
• Hoffman PN, Lasek RJ. Axonal transport of the cytoskeleton in regenerating motor neurons: constancy and change. Brain Res. 1980;202:317–333.
   PubMed Web of Science ®Google Scholar
• Zhou B, Yu P, Lin M-Y, et al. Facilitation of axon regeneration by enhancing mitochondrial transport and rescuing energy deficits. J Cell Biol. 2016;214:103–119.
   PubMed Web of Science ®Google Scholar
• Kim J-Y, Woo S-Y, Hong YB, et al. HDAC6 inhibitors rescued the defective axonal mitochondrial movement in motor neurons derived from the induced pluripotent stem cells of peripheral neuropathy patients with HSPB1 mutation. Stem Cells Int [Internet]. 2016;2016:1–14. Available from: https://www.hindawi.com/journals/sci/2016/9475981/
   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 [Internet]. 2008;28:1688–1701. doi:10.1128/MCB.01154-06.
   PubMed Web of Science ®Google Scholar
• Fukada M, Hanai A, Nakayama A, et al. Loss of deacetylation activity of Hdac6 affects emotional behavior in mice. PLoS One. 2012;7:1–8.
   Web of Science ®Google Scholar
• Pandey UB, Nie Z, Batlevi Y, et al. HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature. 2007/06/15. 2007;447:859–863.
   PubMed Web of Science ®Google Scholar
• Simon D, Laloo B, Barillot M, et al. A mutation in the 3′-UTR of the HDAC6 gene abolishing the post-transcriptional regulation mediated by hsa-miR-433 is linked to a new form of dominant X-linked chondrodysplasia. Hum. Mol. Genet. 2010;19:2015–2027.
   PubMed Web of Science ®Google Scholar
• Butler KV, Kalin J, Brochier C, et al. Rational design and simple chemistry yield a superior, neuroprotective HDAC6 inhibitor. Tubastatin A. 2010;132(31):10842–10846.
   Google Scholar