Premium
Residues phosphorylated by TFIIH are required for E2F‐1 degradation during S‐phase
Author(s) -
Vandel Laurence,
Kouzarides Tony
Publication year - 1999
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/18.15.4280
Subject(s) - transcription factor ii h , e2f , biology , phosphorylation , microbiology and biotechnology , transcription factor , cyclin dependent kinase 7 , transcription (linguistics) , biochemistry , dna repair , protein kinase a , dna , cyclin dependent kinase 2 , gene , nucleotide excision repair , linguistics , philosophy
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.