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
• 来源期刊: 分子细胞生物学报（英文版）
• 年，卷（期）: 2021,（2）
• 所属期刊栏目: Articles
• 页码范围: 91-103
• 页数: 13页
• 语种: 英文
• DOI: 10.1093/jmcb/mjaa076

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 1304 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 SUM01 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.