Interaction between ubiquitin–protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-05

AUTHORS

A. Marti, C. Wirbelauer, M. Scheffner, W. Krek

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 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. More... »

PAGES

14-19

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/8984

DOI

http://dx.doi.org/10.1038/8984

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1050768934

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10559858


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