The retinoblastoma gene product regulates progression through the G1 phase of the cell cycle

  title={The retinoblastoma gene product regulates progression through the G1 phase of the cell cycle},
  author={David W. Goodrich and Nan Wang and Yue-wei Qian and Eva Y.-H. P. Lee and Wen-Hwa Lee},
Inhibition of DNA synthesis by RB: effects on G1/S transition and S-phase progression.
Results suggest that continued phosphorylation of RB beyond G1/S is required for the completion of DNA replication, and reveal a novel role for RB in the inhibition of S-phase progression that is distinct from the inhibited of the G1-S transition.
Overproduction of Rb protein after the G1/S boundary causes G2 arrest
Results indicate that Rb protein is interacting with some component(s) of the cell cycle-regulatory machinery during G2 phase.
Regulation of the p21Sdi1/Cip1/Waf1 DNA Synthesis Inhibitor in Senescent Human Diploid Fibroblasts
It is suggested that the inability of mitogen-stimulated senescent cells to down-regulate p21Sdi1 levels contributes to the resulting lack of late Gi gene expression and failure to traverse the G1/S phase boundary.
Role of the retinoblastoma protein in cell cycle arrest mediated by a novel cell surface proliferation inhibitor
A novel cell regulatory sialoglycopeptide (CeReS‐18), purified from the cell surface of bovine cerebral cortex cells has been shown to be a potent and reversible inhibitor of proliferation of a wide
Abrogation by c-myc of Gl phase arrest induced by RB protein but not by p53
Co-injection of c-myc, but not EJ-ras, c-fos or c-jun, inhibits the ability of Rb to arrest the cell cycle, and c- myc and RB specifically antagonize one another in the cell.
Regulation of Cellular Genes in a Chromosomal Context by the Retinoblastoma Tumor Suppressor Protein
The results indicate that pRb is involved in the transcriptional downregulation of the E2F-1, E2f-2, dihydrofolate reductase, thymidine kinase, c-myc, proliferating-cell nuclear antigen, p107, and p21/Cip1 genes, and suggest that it plays a role in downregulating the immediate-early gene response to serum stimulation.
A retinoblastoma-binding protein that affects cell-cycle control and confers transforming ability
A new gene, Bog (for B5T over-expressed gene), which was identified and shown to be overexpressed in several transformed rat liver epithelial (RLE) cell lines resistant to the growth-inhibitory effect of TGF-ß1, as well as in primary human liver tumours, is described.
The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein.
It is demonstrated that Id-2 expression was able to reverse the inhibition of cellular proliferation and the block in cell cycle progression mediated by the product of the retinoblastoma tumor suppressor gene pRB, suggesting that the interaction between Id-1 and pRB is a molecular pathway over which synchronous changes in growth and differentiation are mediated in vivo.


Retinoblastoma cancer suppressor gene product is a substrate of the cell cycle regulator cdc2 kinase.
Results indicate that cdc2 or a kinase with similar substrate specificity is involved in the cell cycle‐dependent phosphorylation of the RB protein.
A cellular protein that competes with SV40 T antigen for binding to the retinoblastoma gene product
Two lines of evidence support the notion that RbAP46 and simian virus 40 T antigen have homologous Rb-binding properties and suggest that endogenous cellular proteins might exist that bind to the same regions of Rb and thereby mediate its function.
Adenovirus E1a prevents the retinoblastoma gene product from complexing with a cellular transcription factor
It is demonstrated that the Rb protein forms a complex with a DNA-bound transcription factor, and suggests that theRb protein might act by regulating transcription, which is thought to inactivate the growth-suppressing properties of the R b protein.
Hyperphosphorylation of the retinoblastoma gene product is determined by domains outside the simian virus 40 large-T-antigen-binding regions
It is demonstrated that the domains in pRB responsible for binding to large T are distinct from those recognized by the relevant pRB-specific kinase(s) and/or those which contain cell cycle-dependent phosphorylation sites.
Expression of the human retinoblastoma gene product pp110RB in insect cells using the baculovirus system.
The availability of soluble, intact, and presumably active pp110RB in large quantity represents a significant advance for studying the biochemical and biophysical properties of the RB gene product as well as its potential biological function in cancer suppression.
The molecular basis of cancer suppression by the retinoblastoma gene.
  • W. Lee
  • Biology
    Princess Takamatsu symposia
  • 1989
It is observed that RB protein phosphorylation oscillates with cell-cycle and the unphosphorylated form is present predominantly in the G0/G1 phase, suggesting that RBprotein was modulated through phosphorylated, may play an important role in these cellular functions.