SUMOylation of α-tubulin is a novel modification regulating microtubule dynamics  

作　　者：Wenfeng Feng Rong Liu Xuan Xie Lei Diao Nannan Gao Jinke Cheng Xu Zhang Yong Li Lan Bao 

机构地区：[1]State Key Laboratory of Cell Biology,CAS Center for Excellence in Molecular Cell Science/Shanghai Institute of Biochemistry and Cell Biology,University of Chinese Academy of Sciences,Chinese Academy of Sciences,Shanghai 200031,China [2]Institute of Brain-Intelligence Technology,Zhangjiang Laboratory,Shanghai Research Center for Brain Science&Brain-Inspired Intelligence,Shanghai 201210,China [3]Discipline of Neuroscience and Department of Biochemistry,Collaborative Innovation Center for Brain Science,Shanghai Jiao Tong University School of Medicine,Shanghai 200025,China [4]Institute of Neuroscience and State Key Laboratory of Neuroscience,CAS Center for Excellence in Brain Science,Chinese Academy of Sciences,Shanghai 200031,China [5]School of Life Science and Technology,ShanghaiTech University,Shanghai 201210,China

出　　处：《Journal of Molecular Cell Biology》2021年第2期91-103,共13页分子细胞生物学报（英文版）

基　　金：This work was supported by grants from the National Natural Science Foundation of China(31991194 and 31330046);the Strategic Priority Research Program of the Chinese Academy of Sciences(XDB19000000);Shanghai Science and Technology Committee(18JC1420301).

摘　　要：Microtubules (MTs) are regulated by a number of known posttranslational modifications (PTMs) on α/β-tubulin to fulfill diverse cellular functions. Here, we showed that SUMOylation is a novel PTM on α-tubulin in vivo and in vitro. The SUMOylation on α-tubulin mainly occurred at Lys 96 (K96), K166, and K304 of soluble α-tubulin and could be removed by small ubiquitin-related modifier (SUMO)-specific peptidase 1. In vitro experiments showed that tubulin SUMOylation could reduce interprotofilament interaction, promote MT catastrophe, and impede MT polymerization. In cells, mutation of the SUMOylation sites on α-tubulin reduced catastrophe frequency and increased the proportion of polymerized α-tubulin, while upregulation of SUMOylation with fusion of SUMO1 reduced α-tubulin assembly into MTs. Additionally, overexpression of SUMOylation-deficient α-tubulin attenuated the neurite extension in Neuro-2a cells. Thus, SUMOylation on α-tubulin represents a new player in the regulation of MT properties.

关 键 词：Α-TUBULIN SUMOYLATION microtubule dynamics microtubule assembly 

分 类 号：Q51[生物学—生物化学]