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The protein NuMA localizes to mitotic spindle poles where it contributes to the organization of microtubules. In this study, we demonstrate that NuMA loses its stable association with the spindle poles after anaphase onset. Using extracts from Xenopus laevis eggs, we show that NuMA is dephosphorylated in anaphase and released from dynein and dynactin. In the presence of a nondegradable form of cyclin B (Delta90), NuMA remains phosphorylated and associated with dynein and dynactin, and remains localized to stable spindle poles that fail to disassemble at the end of mitosis. Inhibition of NuMA or dynein allows completion of mitosis, despite inducing spindle pole abnormalities. We propose that NuMA functions early in mitosis during the formation of spindle poles, but is released from the spindle after anaphase, to allow spindle disassembly and remodelling of the microtubule network.

Original publication

DOI

10.1038/sj.embor.7400046

Type

Journal article

Journal

EMBO Rep

Publication Date

01/2004

Volume

5

Pages

97 - 103

Keywords

Anaphase, Animals, Cold Temperature, Cyclin B, Dynactin Complex, Dyneins, HeLa Cells, Humans, Immunoprecipitation, Microinjections, Microtubule-Associated Proteins, Microtubules, Nuclear Proteins, Spindle Apparatus, Xenopus Proteins, Xenopus laevis