Highlights • The Rod-Zw10-Zwilch complex is required for kinetochore expansion in human cells • Over-expression of the RZZ subunit Rod promotes expansion of unattached kinetochores • C. elegans RZZ is capable of reversible self-assembly into micrometer-scale filaments • A minimal C. elegans Rod-Zw10 complex is sufficient for self ...

2018年11月5日 · Here, we present evidence that kinetochore expansion is driven by oligomerization of the Rod-Zw10-Zwilch (RZZ) complex, an outer kinetochore component that recruits the motor dynein and the SAC proteins Mad1-Mad2.

2022年4月4日 · The new structure explains how intermolecular interactions of the subunits promote the assembly of the RZZ complex; it also explains how RZZ interacts with the farnesyl moiety of Spindly; finally, it sets the basis for understanding how RZZ assembles into supramolecular struc-tures in the corona.

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Kinetochore expansion is an example of protein co-polymerization, but the mechanism is not understood. Here, we present evidence that kinetochore expansion is driven by oligomerization of the Rod-Zw10-Zwilch (RZZ) complex, an outer kinetochore component that recruits the motor dynein and the SAC proteins Mad1-Mad2.

2009年5月8日 · Recent studies have shown that Rod is a significant component of the mitotic checkpoint. It can form the RZZ complex with Zw10 and Zwilch, which plays an important role in maintaining a functional spindle assembly checkpoint. 中文翻译：

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2010年5月12日 · The RZZ complex recruits dynein to kinetochores. We investigated structure, topology, and interactions of the RZZ subunits (ROD, ZWILCH, and ZW10) in vitro, in vivo, and in silico. We identify neuroblastoma-amplified gene (NAG), a ZW10 binder, as a ROD homolog. ROD and NAG contain an N-terminal beta …

2018年11月5日 · We used genome editing to eliminate Bub1, KNL1, and the Rod-Zw10-Zwilch (RZZ) complex in human cells. We show that RZZ’s sole role in SAC activation is to tether Mad1-Mad2 to kinetochores. Separately, Mps1 kinase triggers fibrous corona formation by phosphorylating two N-terminal sites on Rod.