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- Title
Interaction between ubiquitin?protein ligase SCF<sup>SKP2</sup> and E2F-1 underlies the regulation of E2F-1 degradation.
- Authors
Marti, A.; Wirbelauer, C.; Scheffner, M.; Krek, W.
- Abstract
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 p45[SUPSKP2], which is the cell-cycle-regulated component of the ubiquitin-protein ligase SCF[SUPSKP2] that recognizes substrates for this ligase. Disruption of the interaction between E2F-1 and p45[SUPSKP2] 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 SCF[SUPSKP2]-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 SCF(SKP2)and cell-cycle-dependent gene control.
- Publication
Nature Cell Biology, 1999, Vol 1, Issue 1, p14
- ISSN
1465-7392
- Publication type
Academic Journal
- DOI
10.1038/8984