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MTs are regulated by different forms of post-translational modification including acetylation; acetylated MTs represent a more stable microtubule population. In our previous study, we show that inhibition of histone deacetylase 6 (HDAC6), which deacetylates tubulin at lysine 40, rescues defects in MTs and in neuromuscular junction growth caused by tau overexpression. However, HDAC6 also acts on other proteins that involve in distinct biological processes unrelated to tubulins. In order to directly examine the role of increased tubulin acetylation against tau toxicity, we generated site-directed \u03b1-tubulinK40Q mutation by the CRISPR\/Cas9 technology to mimic the acetylated MTs and found that acetylation-mimicking \u03b1-tubulin rescued tau-induced MT defects and neuromuscular junction developmental abnormalities. We also showed that late administration of ACY-1215 and tubastatin A, two potent and selective inhibitors of HDAC6, rescued the tau-induced MT defects after the abnormalities had already become apparent. Our results together indicate that increased MT acetylation by either genetic manipulations or drugs might be used as potential strategies for intervening tauopathies.<\/jats:p>","DOI":"10.1242\/dmm.028316","type":"journal-article","created":{"date-parts":[[2017,8,18]],"date-time":"2017-08-18T00:10:16Z","timestamp":1503015016000},"source":"Crossref","is-referenced-by-count":25,"title":["Increased acetylation of microtubules rescues human tau-induced microtubule defects and neuromuscular junction abnormalities in <i>Drosophila<\/i>"],"prefix":"10.1242","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0220-4141","authenticated-orcid":false,"given":"Chuan-Xi","family":"Mao","sequence":"first","affiliation":[{"name":"Key Laboratory of Molecular and Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xue","family":"Wen","sequence":"additional","affiliation":[{"name":"College of Life Science, Hubei University, Wuhan, Hubei 430062, China"},{"name":"Hubei Collaborative Innovation Center for Green Transformation of Bio-Resources, Hubei University, Wuhan, Hubei 430062, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shan","family":"Jin","sequence":"additional","affiliation":[{"name":"College of Life Science, Hubei University, Wuhan, Hubei 430062, China"},{"name":"Hubei Collaborative Innovation Center for Green Transformation of Bio-Resources, Hubei University, Wuhan, Hubei 430062, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yong Q.","family":"Zhang","sequence":"additional","affiliation":[{"name":"Key Laboratory of Molecular and Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China"},{"name":"University of the Chinese Academy of Sciences, Beijing 100049, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2017,1,1]]},"reference":[{"key":"2021042423584322600_DMM028316C1","doi-asserted-by":"publisher","first-page":"1854","DOI":"10.1091\/mbc.E13-10-0609","article-title":"Alpha-tubulin K40 acetylation is required for contact inhibition of proliferation and cell-substrate adhesion","volume":"25","author":"Aguilar","year":"2014","journal-title":"Mol. 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