Cyclin-B1-mediated inhibition of excess separase is required for timely chromosome disjunction
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چکیده
منابع مشابه
Cyclin-B1-mediated inhibition of excess separase is required for timely chromosome disjunction.
Separase, the cysteine protease that cleaves cohesin and thereby triggers chromosome disjunction, is inhibited by both securin- and phosphorylation-dependent cyclin B1 binding. Using a novel phosphorylation-specific antibody, we show that mitotic-specific phosphorylation of human separase on S1126 is required to establish, but not maintain, cyclin B1 binding. Cells expressing a non-phosphorylat...
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The caspase family protease, separase, is required at anaphase onset to cleave the cohesin complex, which joins sister chromatids. However, among eukaryotes, separases have acquired novel functions. Here, we show that Arabidopsis thaliana radially swollen 4 (rsw4), a temperature-sensitive mutant isolated previously on the basis of root swelling, harbors a mutation in At4g22970, the A. thaliana ...
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Spatially controlled release of sister chromatid cohesion during progression through the meiotic divisions is of paramount importance for error-free chromosome segregation during meiosis. Cohesion is mediated by the cohesin protein complex and cleavage of one of its subunits by the endoprotease separase removes cohesin first from chromosome arms during exit from meiosis I and later from the per...
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Separase is a protease whose liberation from its inhibitory chaperone Securin triggers sister chromatid disjunction at anaphase onset in yeast by cleaving cohesin's kleisin subunit. We have created conditional knockout alleles of the mouse Separase and Securin genes. Deletion of both copies of Separase but not Securin causes embryonic lethality. Loss of Securin reduces Separase activity because...
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ژورنال
عنوان ژورنال: Journal of Cell Science
سال: 2006
ISSN: 1477-9137,0021-9533
DOI: 10.1242/jcs.03083