Publikation: Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation
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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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MARTI, Alain, Christopher WIRBELAUER, Martin SCHEFFNER, Wilhelm KREK, 1999. Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation. In: Nature cell biology. 1999, 1(1), pp. 14-19. ISSN 1465-7392. eISSN 1476-4679. Available under: doi: 10.1038/8984BibTex
@article{Marti1999Inter-42761, year={1999}, doi={10.1038/8984}, title={Interaction between ubiquitin-protein ligase SCF<sup>SKP2</sup> and E2F-1 underlies the regulation of E2F-1 degradation}, number={1}, volume={1}, issn={1465-7392}, journal={Nature cell biology}, pages={14--19}, author={Marti, Alain and Wirbelauer, Christopher and Scheffner, Martin and Krek, Wilhelm} }
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