Pubblicazione scientifica

Structural Basis for Mitotic Centrosome Assembly in Flies

FILONE TECNOLOGICO	TEMA
produzione e cattura

RIASSUNTO

Summary

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.

DATA

Data di pubblicazione: 01/06/2017

AUTORI

FENG ZHE
CABALLE ANNA
WAINMAN ALAN
JOHNSON STEVEN
HAENSELE ANDREAS FM
COTTEE MATTHEW A
CONDUIT PAUL T
LEA SUSAN M
RAFF JORDAN W

ENTE DI AFFERENZA

SIR WILLIAM DUNN SCHOOL OF PATHOLOGY UNIV OXFORD SOUTH

RIVISTA

Cell, 169(6), 1078-1089.e13

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