posted on 2015-08-07, 00:00authored byNingning Liu, Yun Xiong, Yiran Ren, Linlin Zhang, Xianfei He, Xincheng Wang, Min Liu, Dengwen Li, Wenqing Shui, Jun Zhou
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.