α-Tubulin acetylation at lysine 40 regulates dendritic arborization and larval locomotion by promoting microtubule stability in Drosophila.

α-Tubulin acetylation at lysine 40 regulates dendritic arborization and larval locomotion by promoting microtubule stability in Drosophila.
复制标题

赖氨酸 40 处的 α-微管蛋白乙酰化通过促进果蝇微管稳定性来调节树突分枝和幼虫运动

DOI:
10.1371/journal.pone.0280573
复制
发表时间:
2023
期刊:
影响因子:
3.7
通讯作者:
Shan, Jin
Shan, Jin
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Niu, Xiaoxiao;Mao, Chuan-Xi;Wang, Shan;Wang, Xiongxiong;Zhang, Youyu;Hu, Juncheng;Bi, Ran;Liu, Zhihua;Shan, Jin

文献摘要

参考文献

相似文献

小管蛋白的翻译后修饰会增加微管蛋白的动态复杂性和功能多样性。 yltransferase,并通过突变Lys-40进行arg α1微管蛋白。 Ulin脱乙酰化通过降低稳定性而损害了树突状形态微管蛋白使用延时记录,我们发现ATAT和α1-tubulink40r突变大大增加了可能是未成熟的树突状蛋白的数量确定神经元发展和功能。
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 developmental defects in atat mutants could be reversed by enhancing the stability of microtubules either through knocking down the microtubule severing protein Katanin 60 or through overexpressing tubulin-specific chaperone E, suggesting that α-tubulin deacetylation impairsed dendritic morphology by decreasing the stability of microtubules. Using time-lapse recordings, we found that atat and α1-tubulinK40R mutations dramatically increased the number of dendritic protrusions that were likely to be immature dendritic precursors. Finally, we showed that both Atat and α-tubulin acetylation were required in class I da neurons to control larval locomotion. These findings add novel insight into the current knowledge of the role of α-tubulin acetylation in regulating neuronal development and functions.
DOI: 10.1038/ncomms3532
发表时间: 2013
影响因子: 16.6
作者:
Ageta-Ishihara, Natsumi;Miyata, Takaki;Ohshima, Chika;Watanabe, Masahiko;Sato, Yoshikatsu;Hamamura, Yuki;Higashiyama, Tetsuya;Mazitschek, Ralph;Bito, Haruhiko;Kinoshita, Makoto
通讯作者: Kinoshita, Makoto
DOI: 10.1126/sciadv.aax2705
发表时间: 2019-12-01
期刊: SCIENCE ADVANCES
影响因子: 13.6
作者:
Even, Aviel;Morelli, Giovanni;Nguyen, Laurent
通讯作者: Nguyen, Laurent
DOI: 10.1097/00005072-199609000-00003
发表时间: 1996-09-01
影响因子: 3.2
作者:
Hempen, B;Brion, JP
通讯作者: Brion, JP
DOI: 10.1002/bies.20154
发表时间: 2005-01-01
期刊: BIOESSAYS
影响因子: 4
作者:
Andersen, SSL
通讯作者: Andersen, SSL
DOI: 10.1016/j.cub.2019.12.022
发表时间: 2020-02-24
期刊: CURRENT BIOLOGY
影响因子: 9.2
作者:
Coombes, Courtney E.;Saunders, Harriet A. J.;Gardner, Melissa K.
通讯作者: Gardner, Melissa K.