Journal
JOURNAL OF CELL BIOLOGY
Volume 204, Issue 5, Pages 647-657Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201311015
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Funding
- National Institutes of Health [GM074215]
- Training in Cancer Cell Biology grant (National Institutes of Health-National Cancer Institute) [T32-CA067754]
- National Institutes of Health Predoctoral Genetics Training grant [T32 GM008666]
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Recruitment of Mad1-Mad2 complexes to unattached kinetochores is a central event in spindle checkpoint signaling. Despite its importance, the mechanism that recruits Mad1- Mad2 to kinetochores is unclear. In this paper, we show that MAD-1 interacts with BUB-1 in Caenorhabditis elegans. Mutagenesis identified specific residues in a segment of the MAD-1 coiled coil that mediate the BUB-1 interaction. In addition to unattached kinetochores, MAD-1 localized between separating meiotic chromosomes and to the nuclear periphery. Mutations in the MAD-1 coiled coil that selectively disrupt interaction with BUB-1 eliminated MAD-1 localization to unattached kinetochores and between meiotic chromosomes, both of which require BUB-1, and abrogated checkpoint signaling. The identified MAD-1 coiled-coil segment interacted with a C-terminal region of BUB-1 that contains its kinase domain, and mutations in this region prevented MAD-1 kinetochore targeting independently of kinase activity. These results delineate an interaction between BUB-1 and MAD-1 that targets MAD-1 MAD-2 complexes to kinetochores and is essential for spindle checkpoint signaling.
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