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  • Anaphase-Promoting Complex-Cyclosome  (3)
  • Phosphorylation  (3)
  • 1
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    Anaphase inactivation of the spindle checkpoint (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-07-11
    Description: The spindle checkpoint delays cell cycle progression until microtubules attach each pair of sister chromosomes to opposite poles of the mitotic spindle. Following sister chromatid separation, however, the checkpoint ignores chromosomes whose kinetochores are attached to only one spindle pole, a state that activates the checkpoint prior to metaphase. We demonstrate that, in budding yeast, mutual inhibition between the anaphase-promoting complex (APC) and Mps1, an essential component of the checkpoint, leads to sustained inactivation of the spindle checkpoint. Mps1 protein abundance decreases in anaphase, and Mps1 is a target of the APC. Furthermore, expression of Mps1 in anaphase, or repression of the APC in anaphase, reactivates the spindle checkpoint. This APC-Mps1 feedback circuit allows cells to irreversibly inactivate the checkpoint during anaphase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palframan, William J -- Meehl, Janet B -- Jaspersen, Sue L -- Winey, Mark -- Murray, Andrew W -- GM43987/GM/NIGMS NIH HHS/ -- GM51312/GM/NIGMS NIH HHS/ -- R37 GM043987/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 4;313(5787):680-4. Epub 2006 Jul 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Biological Laboratories, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16825537" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anaphase/*physiology ; Anaphase-Promoting Complex-Cyclosome ; Cdc20 Proteins ; Cell Cycle Proteins/metabolism ; Chromosomes, Fungal/physiology ; Feedback, Physiological ; GTP-Binding Proteins/metabolism ; Kinetochores/physiology ; Mad2 Proteins ; Mitosis ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Protein-Tyrosine Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*cytology/metabolism ; Saccharomyces cerevisiae Proteins/genetics/*metabolism ; Securin ; Spindle Apparatus/*physiology ; Ubiquitin-Protein Ligase Complexes/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Budding yeast Cdc20: a target of the spindle checkpoint (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-07
    Description: The spindle checkpoint regulates the cell division cycle by keeping cells with defective spindles from leaving mitosis. In the two-hybrid system, three proteins that are components of the checkpoint, Mad1, Mad2, and Mad3, were shown to interact with Cdc20, a protein required for exit from mitosis. Mad2 and Mad3 coprecipitated with Cdc20 at all stages of the cell cycle. The binding of Mad2 depended on Mad1 and that of Mad3 on Mad1 and Mad2. Overexpression of Cdc20 allowed cells with a depolymerized spindle or damaged DNA to leave mitosis but did not overcome the arrest caused by unreplicated DNA. Mutants in Cdc20 that were resistant to the spindle checkpoint no longer bound Mad proteins, suggesting that Cdc20 is the target of the spindle checkpoint.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, L H -- Lau, L F -- Smith, D L -- Mistrot, C A -- Hardwick, K G -- Hwang, E S -- Amon, A -- Murray, A W -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):1041-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California at San Francisco, San Francisco, CA 94143-0444, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9461437" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Cadherins ; Calcium-Binding Proteins/metabolism ; *Carrier Proteins ; Cdc20 Proteins ; Cdh1 Proteins ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; DNA Damage ; DNA Replication ; Fungal Proteins/chemistry/*metabolism ; Ligases/metabolism ; Mad2 Proteins ; *Mitosis ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/metabolism ; Phosphoproteins/metabolism ; *Repressor Proteins ; Saccharomyces cerevisiae/*cytology/*metabolism ; *Saccharomyces cerevisiae Proteins ; Spindle Apparatus/*metabolism ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    The centromeric protein Sgo1 is required to sense lack of tension on mitotic chromosomes (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-08
    Description: Chromosome alignment on the mitotic spindle is monitored by the spindle checkpoint. We identify Sgo1, a protein involved in meiotic chromosome cohesion, as a spindle checkpoint component. Budding yeast cells with mutations in SGO1 respond normally to microtubule depolymerization but not to lack of tension at the kinetochore, and they have difficulty attaching sister chromatids to opposite poles of the spindle. Sgo1 is thus required for sensing tension between sister chromatids during mitosis, and its degradation when they separate may prevent cell cycle arrest and chromosome loss in anaphase, a time when sister chromatids are no longer under tension.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Indjeian, Vahan B -- Stern, Bodo M -- Murray, Andrew W -- GM043987/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 7;307(5706):130-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Biological Laboratories, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15637284" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Chromatids/physiology ; Chromosomal Proteins, Non-Histone ; Chromosome Segregation ; Chromosomes, Fungal/*physiology ; Kinetochores/physiology ; *Mitosis ; Mutation ; Nuclear Proteins/genetics/metabolism/*physiology ; Phosphoproteins/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Saccharomyces cerevisiae/genetics/*physiology ; Saccharomyces cerevisiae Proteins/genetics/metabolism/*physiology ; Spindle Apparatus/*physiology ; Ubiquitin-Protein Ligase Complexes/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    How to compact DNA (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murray, A W -- New York, N.Y. -- Science. 1998 Oct 16;282(5388):425, 427.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California at San Francisco, San Francisco, CA 94143-0444, USA. amurray@socrates.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841400" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/chemistry/*metabolism ; Adenosine Triphosphate/metabolism ; Animals ; CDC2 Protein Kinase/metabolism ; Carrier Proteins/metabolism ; *Cell Cycle Proteins ; *Chromosomal Proteins, Non-Histone ; Chromosomes/*metabolism/ultrastructure ; Cyclin B/metabolism ; DNA/chemistry/*metabolism ; DNA, Superhelical/chemistry ; DNA-Binding Proteins/chemistry/*metabolism ; Dosage Compensation, Genetic ; Female ; Interphase ; Male ; *Mitosis ; Multiprotein Complexes ; Nuclear Proteins/metabolism ; Nucleic Acid Conformation ; Phosphorylation ; Xenopus ; *Xenopus Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    Activation of the budding yeast spindle assembly checkpoint without mitotic spindle disruption (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-16
    Description: The spindle assembly checkpoint keeps cells with defective spindles from initiating chromosome segregation. The protein kinase Mps1 phosphorylates the yeast protein Mad1p when this checkpoint is activated, and the overexpression of Mps1p induces modification of Mad1p and arrests wild-type yeast cells in mitosis with morphologically normal spindles. Spindle assembly checkpoint mutants overexpressing Mps1p pass through mitosis without delay and can produce viable progeny, which demonstrates that the arrest of wild-type cells results from inappropriate activation of the checkpoint in cells whose spindle is fully functional. Ectopic activation of cell-cycle checkpoints might be used to exploit the differences in checkpoint status between normal and tumor cells and thus improve the selectivity of chemotherapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hardwick, K G -- Weiss, E -- Luca, F C -- Winey, M -- Murray, A W -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):953-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco, CA 94143-0444, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688079" target="_blank"〉PubMed〈/a〉
    Keywords: *Carrier Proteins ; Cell Cycle ; *Cell Cycle Proteins ; Fungal Proteins/*metabolism ; *Mitosis ; Nuclear Proteins/*metabolism ; Phosphoproteins/*metabolism ; Phosphorylation ; Protein Kinases ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Protein-Tyrosine Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Repressor Proteins ; Saccharomyces cerevisiae/cytology/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Spindle Apparatus/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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