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XB-ART-10162
Cell September 15, 2000; 102 (6): 817-26.

CENP-E as an essential component of the mitotic checkpoint in vitro.

Abrieu A , Kahana JA , Wood KW , Cleveland DW .


Abstract
Accurate chromatid separation is monitored by a checkpoint mechanism that delays anaphase onset until all centromeres are correctly attached to the mitotic spindle. Using Xenopus egg extracts, the kinetochore-associated microtubule motor protein CENP-E is now found to be required for establishing and maintaining this checkpoint. When CENP-E function is disrupted by immunodepletion or antibody addition, extracts fail to arrest in response to spindle damage. Mitotic arrest can be restored by addition of high levels of soluble MAD2, demonstrating that the absence of CENP-E eliminates kinetochore-dependent signaling but not the downstream steps in checkpoint signal transduction. Because it directly binds both to spindle microtubules and to the kinetochore-associated checkpoint kinase BUBR1, CENP-E is a central component in the vertebrate checkpoint that modulates signaling activity in a microtubule-dependent manner.

PubMed ID: 11030625
Article link: Cell

Genes referenced: bub1b cenpe mad2l1



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