Phosphorylation of Cdc20 by Bub1 provides a catalytic mechanism for APC/C inhibition by the spindle checkpoint (Q24311322)

2

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Dilhan Oncel

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She Chen

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Hongtao Yu

Phosphorylation of human MAD1 by the BUB1 kinase in vitro

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language of work or name

English

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publication date

5 November 2004

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published in

Molecular Cell

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volume

16

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issue

3

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page(s)

387-97

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cites work

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Phosphorylation of Cdc20/fizzy negatively regulates the mammalian cyclosome/APC in the mitotic checkpoint

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Waiting for anaphase: Mad2 and the spindle assembly checkpoint

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Regulation of APC-Cdc20 by the spindle checkpoint

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Complex formation between Mad1p, Bub1p and Bub3p is crucial for spindle checkpoint function

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Direct binding of CDC20 protein family members activates the anaphase-promoting complex in mitosis and G1

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The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20

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The anaphase-promoting complex: proteolysis in mitosis and beyond

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Mad2-Independent inhibition of APCCdc20 by the mitotic checkpoint protein BubR1.

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Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells

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Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20

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Phosphorylation of Cdc20 is required for its inhibition by the spindle checkpoint.

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The spindle checkpoint: structural insights into dynamic signalling

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The Mad2 spindle checkpoint protein has two distinct natively folded states

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Phosphorylation and activation of Bub1 on unattached chromosomes facilitate the spindle checkpoint

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The spindle checkpoint, aneuploidy, and cancer

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The checkpoint delaying anaphase in response to chromosome monoorientation is mediated by an inhibitory signal produced by unattached kinetochores

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Regulation of APC activity by phosphorylation and regulatory factors

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Visualization of Mad2 dynamics at kinetochores, along spindle fibers, and at spindle poles in living cells

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Spindle checkpoint protein Bub1 is required for kinetochore localization of Mad1, Mad2, Bub3, and CENP-E, independently of its kinase activity

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Checkpoint inhibition of the APC/C in HeLa cells is mediated by a complex of BUBR1, BUB3, CDC20, and MAD2

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BubR1 is essential for kinetochore localization of other spindle checkpoint proteins and its phosphorylation requires Mad1.

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Checkpoint protein BubR1 acts synergistically with Mad2 to inhibit anaphase-promoting complex

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Mitotic regulation of the APC activator proteins CDC20 and CDH1

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Distinct chromosome segregation roles for spindle checkpoint proteins

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Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint

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Function of Cdc2p-dependent Bub1p phosphorylation and Bub1p kinase activity in the mitotic and meiotic spindle checkpoint

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Mitotic regulation of the human anaphase-promoting complex by phosphorylation

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The anaphase-promoting complex: it's not just for mitosis any more.

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The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation

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The spindle checkpoint requires cyclin-dependent kinase activity

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Segregating sister genomes: the molecular biology of chromosome separation

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How cells get the right chromosomes

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Splitting the chromosome: cutting the ties that bind sister chromatids

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The Saccharomyces cerevisiae checkpoint gene BUB1 encodes a novel protein kinase

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Bub1p kinase activates the Saccharomyces cerevisiae spindle assembly checkpoint

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