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Structural Basis for Mitotic Centrosome Assembly in Flies

DOI: 10.1016/j.cell.2017.05.030 DOI Help

Authors: Zhe Feng (University of Oxford) , Anna Caballe (University of Oxford) , Alan Wainman (University of Oxford) , Steven Johnson (University of Oxford) , Andreas F. M. Haensele (University of Oxford) , Matthew A. Cottee (University of Oxford) , Paul T. Conduit (University of Oxford) , Susan M. Lea (University of Oxford) , Jordan W. Raff (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Cell , VOL 169 , PAGES 1078 - 1089.e13

State: Published (Approved)
Published: June 2017
Diamond Proposal Number(s): 9306 , 12346

Open Access Open Access

Abstract: In flies, Centrosomin (Cnn) forms a phosphorylation-dependent scaffold that recruits proteins to the mitotic centrosome, but how Cnn assembles into a scaffold is unclear. We show that scaffold assembly requires conserved leucine zipper (LZ) and Cnn-motif 2 (CM2) domains that co-assemble into a 2:2 complex in vitro. We solve the crystal structure of the LZ:CM2 complex, revealing that both proteins form helical dimers that assemble into an unusual tetramer. A slightly longer version of the LZ can form micron-scale structures with CM2, whose assembly is stimulated by Plk1 phosphorylation in vitro. Mutating individual residues that perturb LZ:CM2 tetramer assembly perturbs the formation of these micron-scale assemblies in vitro and Cnn-scaffold assembly in vivo. Thus, Cnn molecules have an intrinsic ability to form large, LZ:CM2-interaction-dependent assemblies that are critical for mitotic centrosome assembly. These studies provide the first atomic insight into a molecular interaction required for mitotic centrosome assembly.

Journal Keywords: centrosome; centriole; PCM; Centrosomin; Cnn; Plk1; mitosis

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Other Facilities: PETRA III; ESRF


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