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Aurora-A condensation mediated by BuGZ aids its mitotic centrosome functions
Hui Zheng1,2, Qiaoqiao Zhang1,2, Xing Liu3
1Laboratory for Aging and Cancer Research, Frontiers Science Center Disease-related Molecular Network, State Key Laboratory of Respiratory Health and Multimorbidity and National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University, Chengdu 610041, Sichuan, China.
Iscience
|May 15, 2024
Summary
Aurora-A kinase undergoes liquid-liquid phase separation (LLPS) at centrosomes during mitosis. This LLPS, influenced by its disordered region and intramolecular interactions, impacts centrosome maturation and spindle formation, with BuGZ enhancing these functions.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Centrosomes, crucial for microtubule organization, are composed of centrioles and pericentriolar material (PCM).
- Liquid-liquid phase separation (LLPS) is increasingly recognized as a mechanism for organizing proteins within the cell, including some centrosomal proteins.
- The role of centrosomal kinases in LLPS during mitosis remains largely unexplored.
Purpose of the Study:
- To investigate whether centrosomal kinases, specifically Aurora-A, undergo phase separation during mitosis.
- To elucidate the mechanisms underlying Aurora-A phase separation and its functional consequences at the centrosome.
- To explore the interaction between Aurora-A and BuGZ in regulating centrosome functions via LLPS.
Main Methods:
- In vitro phase separation assays for Aurora-A.
- Microscopy studies of Aurora-A localization and behavior in centrosomes during prophase.
- Analysis of Aurora-A's intrinsic disordered region (IDR) and intramolecular interactions.
- Investigation of Aurora-A's kinase activity and centrosome functions.
- Co-immunoprecipitation and functional assays involving Aurora-A and BuGZ.
Main Results:
- Aurora-A kinase undergoes liquid-liquid phase separation (LLPS) both in vitro and within centrosomes starting from prophase.
- Aurora-A LLPS is mediated by conserved positively charged residues in its intrinsic disordered region (IDR) and intramolecular N- and C-terminus interactions.
- Aurora-A condensation impacts key centrosome functions, including maturation, separation, and initial spindle formation.
- Aurora-A's kinase activity is modulated by its phase-separated state.
- BuGZ protein interacts with Aurora-A, enhancing its LLPS and thereby promoting centrosome functions.
Conclusions:
- Aurora-A kinase utilizes LLPS at centrosomes during mitosis, regulated by its IDR and intramolecular interactions.
- Aurora-A LLPS is essential for proper centrosome maturation, separation, and spindle assembly.
- Aurora-A and BuGZ cooperate through LLPS to control critical centrosome-dependent functions from prophase onwards.
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