Format

Send to

Choose Destination

See 1 citation found by title matching your search:

J Cell Biol. 2018 Jan 2;217(1):107-116. doi: 10.1083/jcb.201706103. Epub 2017 Oct 26.

Aurora A activation in mitosis promoted by BuGZ.

Author information

1
Department of Embryology, Carnegie Institution for Science, Baltimore, MD.
2
Institute of Basic Medical Sciences, National Center of Biomedical Analysis, Beijing, China.
3
Medical Sciences Program, Indiana University, Bloomington, IN.
4
Institut de Génétique et Développement de Rennes, Equipe laboratoryélisée Ligue Nationale Contre la Cancer 2014-2017, Centre National de la Recherche Scientifique, Université Rennes 1, Rennes, France.
5
State Key Laboratory of Cell Biology, Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.
6
Department of Embryology, Carnegie Institution for Science, Baltimore, MD zheng@ciwemb.edu.

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.

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center