Liu, Ningning Xiong, Yun Ren, Yiran Zhang, Linlin He, Xianfei Wang, Xincheng Liu, Min Li, Dengwen Shui, Wenqing Zhou, Jun Proteomic Profiling and Functional Characterization of Multiple Post-Translational Modifications of Tubulin Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs). However, more conventional PTMs of tubulin and their roles in the regulation of microtubule properties and functions remain poorly defined. Here, we report the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and <i>O</i>-GlcNAcylation in HeLa cells with a proteomic approach. Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys. By using a series of PTM-deficient or PTM-mimicking mutants, we further find that tubulin phosphorylation and acetylation play important roles in the control of microtubule assembly and stability. In addition, these tubulin PTMs have distinct effects on the retrograde transport of adenoviruses along microtubules. These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions. tubulin PTMs;CTT;microtubule;role;tubulin phosphorylation;24 novel PTM sites 2015-08-07
    https://acs.figshare.com/articles/journal_contribution/Proteomic_Profiling_and_Functional_Characterization_of_Multiple_Post_Translational_Modifications_of_Tubulin/2143306
10.1021/acs.jproteome.5b00308.s002