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Volumn 8, Issue 6, 1996, Pages 773-780

The spindle assembly checkpoint

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE;

EID: 0030561511     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80077-9     Document Type: Article
Times cited : (321)

References (74)
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    • labeled epitope, localizes to kinetochores that have attached to the spindle. This paper provides the first evidence that checkpoint components are conserved from yeast to vertebrates, and also suggests that the budding yeast checkpoint components may reside at the kinetochore too. of outstanding interest
    • Chen R-H, Waters JC, Salmon ED, Murray AW. Association of spindle assembly checkpoint component XMAD2 with unattached kinetochores. of outstanding interest Science. 1996; XMAD2, the Xenopus homolog of Mad2, is required for maintenance of the spindle assembly checkpoint in Xenopus egg extracts. XMAD2, like the 3F3/2-labeled epitope, localizes to kinetochores that have attached to the spindle. This paper provides the first evidence that checkpoint components are conserved from yeast to vertebrates, and also suggests that the budding yeast checkpoint components may reside at the kinetochore too.
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    • of outstanding interest. of special interest. This paper describes the cloning of MAD1 and its interesting localization, and shows that Mad1 is hyperphosphorylated when the checkpoint is activated. Mad1 hyperphosphorylation requires BUB1, BUB3 and MAD2, but not BUB2 and MAD3. A crude biochemical pathway can be created from these data and those found in [9].
    • of outstanding interest Hardwick K, Murray AW. Mad1p, a phosphoprotein component of the spindle assembly checkpoint in budding yeast. of special interest J Cell Biol. 131:1995;709-720 This paper describes the cloning of MAD1 and its interesting localization, and shows that Mad1 is hyperphosphorylated when the checkpoint is activated. Mad1 hyperphosphorylation requires BUB1, BUB3 and MAD2, but not BUB2 and MAD3. A crude biochemical pathway can be created from these data and those found in [9].
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    • of special interest. This paper suggests that p53 is a component of the spindle assembly checkpoint in animal cells. Note that both wild-type and p53-mutant cells arrest poorly in nocodazole, suggesting that a different checkpoint defect may lead to the increase in ploidy of the p53-deficient cells.
    • Cross SM, Sanchez CA, Morgan CA, Schimke MK, Ramel S, Idzerda RL, Raskind WH, Reid BJ. A p53-dependent mouse spindle checkpoint. of special interest Science. 267:1995;1353-1356 This paper suggests that p53 is a component of the spindle assembly checkpoint in animal cells. Note that both wild-type and p53-mutant cells arrest poorly in nocodazole, suggesting that a different checkpoint defect may lead to the increase in ploidy of the p53-deficient cells.
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    • Pds1p, an inhibitor of anaphase in budding yeast, plays a critical role in the APC And checkpoint pathway(s)
    • of special interest. This paper and [43] identify Pds1 as a protein that regulates sister chromatid separation. pds1 mutants prematurely separate their sister chromatids, and have defects in the DNA-damage checkpoint and in spindle elongation. As expected, the Pds1 protein is degraded as cells exist mitosis and contains a putative cyclin-destruction box.
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    • of special interest. See annotation [42].
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    • of outstanding interest. Cut2 is required for sister chromatid separation, is degraded as cells exit mitosis and contains a cyclin-destruction box. Truncating Cut2 makes it nondegradable, and replacing the amino terminus with the amino terminus of Cdc13 (fission yeast cyclin B) allows the chimera to be degraded properly and complements a cut2 mutant. Paradoxically, cut2 mutants and cells containing nondegradable Cut2 have the same phenotype, suggesting that Cut2 may bave two roles in sister chromatid separation: its presence is required to license sisters for separation and its destruction is required to initiate separation. Pds1 and Cut2 share limited homology and may be functional homologs.
    • Funabiki H, Yamano H, Kumada K, Nagao K, Hunt T, Yangida M. Cut2 proteolysis required for sister-chromatid separation in fission yeast. of outstanding interest Nature. 381:1996;438-441 Cut2 is required for sister chromatid separation, is degraded as cells exit mitosis and contains a cyclin-destruction box. Truncating Cut2 makes it nondegradable, and replacing the amino terminus with the amino terminus of Cdc13 (fission yeast cyclin B) allows the chimera to be degraded properly and complements a cut2 mutant. Paradoxically, cut2 mutants and cells containing nondegradable Cut2 have the same phenotype, suggesting that Cut2 may bave two roles in sister chromatid separation: its presence is required to license sisters for separation and its destruction is required to initiate separation. Pds1 and Cut2 share limited homology and may be functional homologs.
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