10.1021/acs.jproteome.5b00308.s002
Ningning Liu
Ningning
Liu
Yun Xiong
Yun
Xiong
Yiran Ren
Yiran
Ren
Linlin Zhang
Linlin
Zhang
Xianfei He
Xianfei
He
Xincheng Wang
Xincheng
Wang
Min Liu
Min
Liu
Dengwen Li
Dengwen
Li
Wenqing Shui
Wenqing
Shui
Jun Zhou
Jun
Zhou
Proteomic Profiling
and Functional Characterization
of Multiple Post-Translational Modifications of Tubulin
American Chemical Society
2015
tubulin PTMs
CTT
microtubule
role
tubulin phosphorylation
24 novel PTM sites
2015-08-07 00:00:00
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Proteomic_Profiling_and_Functional_Characterization_of_Multiple_Post_Translational_Modifications_of_Tubulin/2143306
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.