Journal
CELL
Volume 115, Issue 3, Pages 355-367Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(03)00815-8
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Spindle disassembly at the end of mitosis is a complex and poorly understood process. Here, we report that the AAA-ATPase Cdc48/p97 and its adapters Ufd1-Np14, which have a well-established role in membrane functions, also regulate spindle disassembly by modulating microtubule dynamics and bundling at the end of mitosis. In the absence of p97-Ufd1-Np14 function, microtubules in Xenopus egg extracts remain as monopolar spindles attached to condensed chromosomes after Cdc2 kinase activity has returned to the interphase level. Consequently, interphase microtubule arrays and nuclei are not established. Genetic analyses of Cdc48, the yeast homolog of p97, reveal that Cdc48 is also required for disassembly of mitotic spindles after execution of the mitotic exit pathway. Furthermore, Cdc48/p97-Ufd1-Np14 directly binds to spindle assembly factors and regulates their interaction with microtubules at the end of mitosis. Therefore, Cdc48/p97-Ufd1-Np14 is an essential chaperone that regulates transformation of the microtubule structure as cells reenter interphase.
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