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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1999-12-7
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pubmed:abstractText |
The transcription factor E2F-1 is important in the control of cell proliferation. Its activity must be tightly regulated in a cell-cycle-dependent manner to enable programs of gene expression to be coupled closely with cell-cycle position. Here we show that, following its accumulation in the late G1 phase of the cell cycle, E2F-1 is rapidly degraded in S/G2 phase. This event is linked to a specific interaction of E2F-1 with the F-box-containing protein p45SKP2, which is the cell-cycle-regulated component of the ubiquitin-protein ligase SCFSKP2 that recognizes substrates for this ligase. Disruption of the interaction between E2F-1 and p45SKP2 results in a reduction in ubiquitination of E2F-1 and the stabilization and accumulation of transcriptionally active E2F-1 protein. These results indicate that an SCFSKP2-dependent ubiquitination pathway may be involved in the downregulation of E2F-1 activity in the S/G2 phase of the cell cycle, and suggest a link between SCFSKP2 and cell-cycle-dependent gene control.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arid4a protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/E2F Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/E2F1 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/E2F1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/E2f1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma-Binding Protein 1,
http://linkedlifedata.com/resource/pubmed/chemical/S-Phase Kinase-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor DP1,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1465-7392
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10559858-3T3 Cells,
pubmed-meshheading:10559858-Animals,
pubmed-meshheading:10559858-Carrier Proteins,
pubmed-meshheading:10559858-Cell Cycle,
pubmed-meshheading:10559858-Cell Cycle Proteins,
pubmed-meshheading:10559858-Cell Line,
pubmed-meshheading:10559858-DNA-Binding Proteins,
pubmed-meshheading:10559858-E2F Transcription Factors,
pubmed-meshheading:10559858-E2F1 Transcription Factor,
pubmed-meshheading:10559858-G1 Phase,
pubmed-meshheading:10559858-G2 Phase,
pubmed-meshheading:10559858-HeLa Cells,
pubmed-meshheading:10559858-Homeostasis,
pubmed-meshheading:10559858-Humans,
pubmed-meshheading:10559858-Kinetics,
pubmed-meshheading:10559858-Ligases,
pubmed-meshheading:10559858-Mice,
pubmed-meshheading:10559858-Retinoblastoma-Binding Protein 1,
pubmed-meshheading:10559858-S Phase,
pubmed-meshheading:10559858-S-Phase Kinase-Associated Proteins,
pubmed-meshheading:10559858-Substrate Specificity,
pubmed-meshheading:10559858-Transcription Factor DP1,
pubmed-meshheading:10559858-Transcription Factors,
pubmed-meshheading:10559858-Ubiquitin-Protein Ligases,
pubmed-meshheading:10559858-Ubiquitins
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pubmed:year |
1999
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pubmed:articleTitle |
Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation.
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pubmed:affiliation |
Friedrich Miescher Institut, Basel, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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