Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase.

The transcription factor E2F-1 plays a key role in regulating cell cycle progression. Accordingly, E2F-1 activity is itself tightly controlled by a series of transcriptional and post-transcriptional events. Here we show that the E2F-1 activation domain interacts with a kinase activity which phosphorylates two sites, Ser403 and Thr433, within the ...
activation domain. We demonstrate that TFIIH is responsible for the E2F-1 phosphorylation observed in cell extracts and that endogenous E2F-1 interacts in vivo with p62, a component of TFIIH, during S phase. When the two phosphorylation sites in E2F-1 are mutated to alanine, the stability of the E2F-1 activation domain is greatly increased. These results suggest that TFIIH-mediated phosphorylation of E2F-1 plays a role in triggering E2F-1 degradation during S phase.
Mesh Terms:
Amino Acid Sequence, Carrier Proteins, Cell Cycle Proteins, Cell Line, DNA-Binding Proteins, Drosophila Proteins, E2F Transcription Factors, E2F1 Transcription Factor, Hela Cells, Humans, Hydrolysis, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein Kinases, Retinoblastoma-Binding Protein 1, S Phase, Sequence Homology, Amino Acid, Serine, Threonine, Trans-Activators, Transcription Factor DP1, Transcription Factor TFIIH, Transcription Factors, Transcription Factors, TFII, Transcription, Genetic
EMBO J.
Date: Aug. 02, 1999
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