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Cytoskeletal microtubules (MTs) are nucleated from γ-tubulin ring complexes (γTuRCs) located at MT organizing centers (MTOCs), such as the centrosome. However, the exact regulatory mechanism of γTuRC assembly is not fully understood. Here, we showed that the nonreceptor tyrosine kinase c-Abl was associated with and phosphorylated γ-tubulin, the essential component of the γTuRC, mainly on the Y443 residue by in vivo (immunofluorescence and immunoprecipitation) or in vitro (surface plasmon resonance) detection. We further demonstrated that phosphorylation deficiency significantly impaired γTuRC assembly, centrosome construction, and MT nucleation. c-Abl/Arg deletion and γ-tubulin Y443F mutation resulted in an abnormal morphology and compromised spindle function during mitosis, eventually causing uneven chromosome segregation. Our findings reveal that γTuRC assembly and nucleation function are regulated by Abl kinase-mediated γ-tubulin phosphorylation, revealing a fundamental mechanism that contributes to the maintenance of MT function. Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.


Guang-Fei Wang, Qincai Dong, Yu Bai, Jing Gu, Qingping Tao, Junjie Yue, Rui Zhou, Xiayang Niu, Lin Zhu, Caiwei Song, Tong Zheng, Di Wang, Yanwen Jin, Hainan Liu, Cheng Cao, Xuan Liu. c-Abl kinase-mediated phosphorylation of γ-tubulin promotes γ-tubulin ring complexes assembly and microtubule nucleation. The Journal of biological chemistry. 2022 Apr;298(4):101778

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PMID: 35231444

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