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ECB-ART-48412
J Cell Biol 2018 Jan 02;2171:107-116. doi: 10.1083/jcb.201706103.
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Aurora A activation in mitosis promoted by BuGZ.

Huang Y , Li T , Ems-McClung SC , Walczak CE , Prigent C , Zhu X , Zhang X , Zheng Y .


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.

PubMed ID: 29074706
PMC ID: PMC5748987
Article link: J Cell Biol
Grant support: [+]

Genes referenced: LOC115919910 LOC594349 tubgcp2


Article Images: [+] show captions
References [+] :
Bai, A novel mechanism for activation of Aurora-A kinase by Ajuba. 2014, Pubmed