Aurora A activation in mitosis promoted by BuGZ

Yuejia Huang, Teng Li, Stephanie C. Ems-McClung, Claire E. Walczak, Claude Prigent, Xueliang Zhu, Xuemin Zhang, Yixian Zheng

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

Protein phase separation or coacervation has emerged as a potential mechanism to regulate biological functions. We have shown that coacervation of a mostly unstructured protein, BuGZ, promotes assembly of spindle and its matrix. BuGZ in the spindle matrix binds and concentrates tubulin to promote microtubule (MT) assembly. It remains unclear, however, whether BuGZ could regulate additional proteins to promote spindle assembly. In this study, we report that BuGZ promotes Aurora A (AurA) activation in vitro. Depletion of BuGZ in cells reduces the amount of phosphorylated AurA on spindle MTs. BuGZ also enhances MCAK phosphorylation. The two zinc fingers in BuGZ directly bind to the kinase domain of AurA, which allows AurA to incorporate into the coacervates formed by BuGZ in vitro. Importantly, mutant BuGZ that disrupts the coacervation activity in vitro fails to promote AurA phosphorylation in Xenopus laevis egg extracts. These results suggest that BuGZ coacervation promotes AurA activation in mitosis.

Original languageEnglish (US)
Pages (from-to)107-116
Number of pages10
JournalJournal of Cell Biology
Volume217
Issue number1
DOIs
StatePublished - Jan 1 2018

ASJC Scopus subject areas

  • Cell Biology

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    Huang, Y., Li, T., Ems-McClung, S. C., Walczak, C. E., Prigent, C., Zhu, X., Zhang, X., & Zheng, Y. (2018). Aurora A activation in mitosis promoted by BuGZ. Journal of Cell Biology, 217(1), 107-116. https://doi.org/10.1083/jcb.201706103