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Mol Cell. 2010 May 14;38(3):369-82. doi: 10.1016/j.molcel.2010.02.038.

Regulated degradation of spindle assembly factors by the anaphase-promoting complex.

Author information

1
Department of Molecular Cell Biology, University of California, Berkeley, 16 Barker Hall, Berkeley, CA 94720, USA.

Abstract

The ubiquitin ligase anaphase-promoting complex (APC/C) is essential for cell division in all eukaryotes. Loss of APC/C activity arrests cells at metaphase and results in severe aberrations of the mitotic spindle, but how the APC/C regulates spindle formation is not understood. Here, we report that the APC/C promotes the ubiquitination and degradation of four proteins required for Ran-dependent spindle assembly: Bard1, Hmmr, HURP, and NuSAP. Among these substrates, HURP and NuSAP can be degraded during spindle formation when the spindle checkpoint is active. Their degradation requires additional layers of regulation, and both SAFs are only degraded after being released from their inhibitor importin beta by Ran(GTP). Our findings reveal a tightly regulated mechanism by which the APC/C and the GTPase Ran control the abundance of active spindle assembly factors to achieve the accurate formation of the mitotic spindle.

PMID:
20471943
PMCID:
PMC2883244
DOI:
10.1016/j.molcel.2010.02.038
[Indexed for MEDLINE]
Free PMC Article

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