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The A urora B kinase in T rypanosoma brucei undergoes post‐translational modifications and is targeted to various subcellular locations through binding to TbCPC 1
Author(s) -
Hu Huiqing,
Yu Zhonglian,
Liu Yi,
Wang Tao,
Wei Ying,
Li Ziyin
Publication year - 2014
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12458
Subject(s) - cytokinesis , biology , microbiology and biotechnology , trypanosoma brucei , phosphorylation , mitosis , kinase , phosphatase , anaphase , biochemistry , cell cycle , cell division , cell , gene
Summary The chromosomal passenger complex ( CPC ) in animals, consisting of Aurora B kinase and three evolutionarily conserved proteins, plays crucial roles in mitosis and cytokinesis. However, T rypanosoma brucei expresses an unusual CPC consisting of an Aurora‐like kinase, TbAUK 1, and two kinetoplastid‐specific proteins, TbCPC 1 and TbCPC 2. Despite their essential functions, little is known about the regulation of TbAUK 1 and the roles of TbCPC 1 and TbCPC 2. Here, we investigate the effect of post‐translational modification on the activity and spatiotemporal control of TbAUK 1, and demonstrate that phosphorylation of two conserved threonine residues in the activation loop of the kinase domain contributes to TbAUK 1 activation and function. TbAUK 1 is SUMO ylated in vivo , and mutation of the SUMO ‐conjugation site compromises TbAUK 1 function. Degradation of TbAUK 1 requires two destruction boxes and is mediated by the anaphase‐promoting complex/cyclosome ( APC / C ), whereas degradation of TbCPC 1 and TbCPC 2 is not dependent on the predicted destruction boxes and is APC / C ‐independent. Moreover, we determine the domains in CPC subunits that mediate the pairwise interactions, and show that disruption of the interaction impairs the localization of TbAUK 1 and TbCPC 2 but not TbCPC 1. Our results demonstrate the requirement of post‐translational modifications for TbAUK 1 function and a crucial role of TbCPC 1 in mediating TbAUK 1 localization.