Source:http://linkedlifedata.com/resource/pubmed/id/12629549
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2003-4-1
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| pubmed:abstractText |
In the early embryonic cell cycle, Cdc2-cyclin B functions like an autonomous oscillator, whose robust biochemical rhythm continues even when DNA replication or mitosis is blocked. At the core of the oscillator is a negative feedback loop; cyclins accumulate and produce active mitotic Cdc2-cyclin B; Cdc2 activates the anaphase-promoting complex (APC); the APC then promotes cyclin degradation and resets Cdc2 to its inactive, interphase state. Cdc2 regulation also involves positive feedback, with active Cdc2-cyclin B stimulating its activator Cdc25 (refs 5-7) and inactivating its inhibitors Wee1 and Myt1 (refs 8-11). Under the correct circumstances, these positive feedback loops could function as a bistable trigger for mitosis, and oscillators with bistable triggers may be particularly relevant to biological applications such as cell cycle regulation. Therefore, we examined whether Cdc2 activation is bistable. We confirm that the response of Cdc2 to non-degradable cyclin B is temporally abrupt and switch-like, as would be expected if Cdc2 activation were bistable. We also show that Cdc2 activation exhibits hysteresis, a property of bistable systems with particular relevance to biochemical oscillators. These findings help establish the basic systems-level logic of the mitotic oscillator.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CDC2-CDC28 Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Cdk2 protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Extracts,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin B,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
1465-7392
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
5
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
346-51
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:12629549-Animals,
pubmed-meshheading:12629549-Biological Clocks,
pubmed-meshheading:12629549-CDC2-CDC28 Kinases,
pubmed-meshheading:12629549-Cell Cycle,
pubmed-meshheading:12629549-Cell Extracts,
pubmed-meshheading:12629549-Cyclin B,
pubmed-meshheading:12629549-Cyclin-Dependent Kinase 2,
pubmed-meshheading:12629549-Cyclin-Dependent Kinases,
pubmed-meshheading:12629549-Eukaryotic Cells,
pubmed-meshheading:12629549-Feedback, Physiological,
pubmed-meshheading:12629549-Female,
pubmed-meshheading:12629549-Mitosis,
pubmed-meshheading:12629549-Models, Biological,
pubmed-meshheading:12629549-Oocytes,
pubmed-meshheading:12629549-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12629549-Reaction Time,
pubmed-meshheading:12629549-Xenopus Proteins,
pubmed-meshheading:12629549-Xenopus laevis
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| pubmed:year |
2003
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| pubmed:articleTitle |
Building a cell cycle oscillator: hysteresis and bistability in the activation of Cdc2.
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| pubmed:affiliation |
Department of Molecular Pharmacology, Stanford University School of Medicine, Stanford, CA 94305-5174, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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