| Literature DB >> 25987563 |
Si Li1, Zhaoxuan Deng2, Jingyan Fu2, Caiyue Xu2, Guangwei Xin2, Zhige Wu2, Jia Luo2, Gang Wang2, Shuli Zhang2, Boyan Zhang2, Fangdong Zou3, Qing Jiang4, Chuanmao Zhang5.
Abstract
Aurora kinase A and B share great similarity in sequences, structures, and phosphorylation motif, yet they show different localizations and play distinct crucial roles. The factors that determine such differences are largely unknown. Here we targeted Aurora A to the localization of Aurora B and found that Aurora A phosphorylates the substrate of Aurora B and substitutes its function in spindle checkpoint. In return, the centrosome targeting of Aurora B substitutes the function of Aurora A in the mitotic entry. Expressing the chimera proteins of the Auroras with exchanged N termini in cells indicates that the divergent N termini are also important for their spatiotemporal localizations and functions. Collectively, we demonstrate that functional divergence of Aurora kinases is determined by spatial compartmentalization, and their divergent N termini also contribute to their spatial and functional differentiation.Entities:
Keywords: Aurora kinase; INCENP; TPX2; cell cycle; checkpoint control; mitotic spindle; protein kinase; protein phosphorylation; spindle assembly.
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Year: 2015 PMID： 25987563 PMCID： PMC4498088 DOI： 10.1074/jbc.M115.652453
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157