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XB-ART-1399
J Cell Biol September 12, 2005; 170 (6): 873-80.

Microtubule capture by CENP-E silences BubR1-dependent mitotic checkpoint signaling.

Mao Y , Desai A , Cleveland DW .


Abstract
The mitotic checkpoint is the major cell cycle control mechanism for maintaining chromosome content in multicellular organisms. Prevention of premature onset of anaphase requires activation at unattached kinetochores of the BubR1 kinase, which acts with other components to generate a diffusible "stop anaphase" inhibitor. Not only does direct binding of BubR1 to the centromere-associated kinesin family member CENP-E activate its essential kinase, binding of a motorless fragment of CENP-E is shown here to constitutively activate BubR1 bound at kinetochores, producing checkpoint signaling that is not silenced either by spindle microtubule capture or the tension developed at those kinetochores by other components. Using purified BubR1, microtubules, and CENP-E, microtubule capture by the CENP-E motor domain is shown to silence BubR1 kinase activity in a ternary complex of BubR1-CENP-E-microtubule. Together, this reveals that CENP-E is the signal transducing linker responsible for silencing BubR1-dependent mitotic checkpoint signaling through its capture at kinetochores of spindle microtubules.

PubMed ID: 16144904
PMC ID: PMC2171436
Article link: J Cell Biol
Grant support: [+]
Genes referenced: bub1 bub1b cdk1 cenpe mad2l1 mapk1 mxd1 rps27 tbx2


Article Images: [+] show captions
References [+] :
Abrieu, CENP-E as an essential component of the mitotic checkpoint in vitro. 2000, Pubmed, Xenbase


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