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SUMOylation of α-tubulin is a novel modification regulating microtubule dynamics
Wenfeng Feng1,2,† , Rong Liu1,† , Xuan Xie1 , Lei Diao1 , Nannan Gao1 , Jinke Cheng3 , Xu Zhang2,4,5 , Yong Li3 , Lan Bao1,5,*
1State 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
2Institute of Brain-Intelligence Technology, Zhangjiang Laboratory; Shanghai Research Center for Brain Science & Brain-Inspired Intelligence, Shanghai 201210, China
3Discipline of Neuroscience and Department of Biochemistry, Collaborative Innovation Center for Brain Science, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China
4Institute of Neuroscience and State Key Laboratory of Neuroscience, CAS Center for Excellence in Brain Science, Chinese Academy of Sciences, Shanghai 200031, China
5School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China
†These authors contributed equally to this work.
*Correspondence to:Lan Bao , Email:baolan@sibcb.ac.cn
J Mol Cell Biol, Volume 13, Issue 2, February 2021, 91-103,   https://doi.org/10.1093/jmcb/mjaa076
Keyword: α-tubulin, SUMOylation, microtubule dynamics, microtubule assembly

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.


Volume 13, Issue 2
February 2021