TY - JOUR
T1 - Transcriptional inhibition by the retinoblastoma protein.
AU - Fattaey, A
AU - Helin, K
AU - Harlow, E
N1 - Keywords: Adenoviruses, Human; Animals; Carrier Proteins; Cell Cycle; Cell Cycle Proteins; Chloramphenicol O-Acetyltransferase; Cloning, Molecular; DNA; DNA-Binding Proteins; E2F Transcription Factors; E2F1 Transcription Factor; Phosphorylation; Recombinant Fusion Proteins; Retinoblastoma Protein; Trans-Activation (Genetics); Transcription Factor DP1; Transcription Factors; Transcription, Genetic
PY - 1993
Y1 - 1993
N2 - The retinoblastoma protein, pRB, appears to play a key role in coordinating the regulation of cell cycle position and transcriptional events. pRB undergoes specific cell-cycle-dependent phosphorylation, being underphosphorylated in G1 and heavily phosphorylated in S, G2, and M. The underphosphorylated form is able to interact with the E2F transcription factor. Recently, we have cloned a cDNA for E2F-1. By using this clone and a series of non-pRB binding mutants, we have been able to show that the binding of pRB to E2F-1 causes inhibition of E2F-mediated transactivation. pRB's inhibition of E2F-mediated transcription would be lost by mutation in the retinoblastoma gene in human tumours, by pRB's interaction with DNA tumour virus oncoproteins, or by phosphorylation during the cell cycle.
AB - The retinoblastoma protein, pRB, appears to play a key role in coordinating the regulation of cell cycle position and transcriptional events. pRB undergoes specific cell-cycle-dependent phosphorylation, being underphosphorylated in G1 and heavily phosphorylated in S, G2, and M. The underphosphorylated form is able to interact with the E2F transcription factor. Recently, we have cloned a cDNA for E2F-1. By using this clone and a series of non-pRB binding mutants, we have been able to show that the binding of pRB to E2F-1 causes inhibition of E2F-mediated transactivation. pRB's inhibition of E2F-mediated transcription would be lost by mutation in the retinoblastoma gene in human tumours, by pRB's interaction with DNA tumour virus oncoproteins, or by phosphorylation during the cell cycle.
U2 - 10.1098/rstb.1993.0075
DO - 10.1098/rstb.1993.0075
M3 - Journal article
C2 - 8103936
SN - 0962-8436
VL - 340
SP - 333
EP - 336
JO - Philosophical Transactions of the Royal Society of London. Biological Sciences
JF - Philosophical Transactions of the Royal Society of London. Biological Sciences
IS - 1293
ER -