| APC/C-mediated degradation in early mitosis: how to avoid spindle assembly checkpoint inhibition. | |
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MedLine Citation:
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PMID: 16861901 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The APC/C is an E3 ubiquitin ligase that, by targeting substrates for proteasomal degradation, plays a major role in cell cycle control. In complex with one of two WD40 activator proteins, Cdc20 or Cdh1, the APC/C is active from early mitosis through to late G1 and during this time targets many critical regulators of the cell cycle for degradation. However, this destruction is carefully ordered to ensure that cell cycle events are executed in a timely fashion. Recent studies have begun to shed light on how the APC/C selects different substrates at different times in the cell cycle. One particular problem is how the APC/C recognizes its first set of substrates, Nek2A and cyclin A, in early mitosis when, at this time, the spindle assembly checkpoint (SAC) inhibits most APC/C-dependent degradation. The answer may lie in how substrates are recruited to the APC/C. While checkpoint-dependent substrates appear to require Cdc20 for recruitment, experiments on the early mitotic substrate Nek2A demonstrate that it can bind the APC/C in the absence of Cdc20. The direct interaction of substrates with core subunits of the APC/C could allow their degradation to proceed unhindered even when the SAC is active. |
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Authors:
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Andrew M Fry; Hiroyuki Yamano |
Publication Detail:
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Type: Journal Article; Review Date: 2006-07-17 |
Journal Detail:
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Title: Cell cycle (Georgetown, Tex.) Volume: 5 ISSN: 1551-4005 ISO Abbreviation: Cell Cycle Publication Date: 2006 Jul |
Date Detail:
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Created Date: 2006-08-02 Completed Date: 2006-10-04 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101137841 Medline TA: Cell Cycle Country: United States |
Other Details:
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Languages: eng Pagination: 1487-91 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, University of Leicester, Leicester, UK. amf5@le.ac.uk |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cyclins / metabolism* Endopeptidases / metabolism Humans Mitosis* Mitotic Spindle Apparatus Ubiquitin-Protein Ligase Complexes / metabolism* Ubiquitin-Protein Ligases / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Cyclins; EC 3.4.-/Endopeptidases; EC 6.3.2.19/Ubiquitin-Protein Ligase Complexes; EC 6.3.2.19/Ubiquitin-Protein Ligases; EC 6.3.2.19/anaphase-promoting complex |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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