期刊
JOURNAL OF PROTEOME RESEARCH
卷 14, 期 8, 页码 3292-3304出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jproteome.5b00308
关键词
tubulin; post-translational modification; microtubule assembly; microtubule stability; intracellular transport
资金
- National Natural Science Foundation of China [31471262, 31170782, 31401150]
- National Science and Technology Major Project of China [2012ZX10001-006]
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 O-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.
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