The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest

@article{Dunaief1994TheRP,
  title={The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest},
  author={Joshua L. Dunaief and Bruce Strober and Sushovan Guha and Paul A. Khavari and Kimona {\AA}lin and Jeremy Luban and Martin Begemann and Gerald R. Crabtree and Stephen P. Goff},
  journal={Cell},
  year={1994},
  volume={79},
  pages={119-130}
}
High mobility group protein HMGA1 inhibits retinoblastoma protein‐mediated cellular G0 arrest
TLDR
It is reported that RB interacts with the high mobility group protein A1 (HMGA1), a‐non‐histone architectural chromatin factor that is frequently overexpressed in cancer cells, and HMGA1 binds the small pocket domain of RB, and competes with HDAC1.
Tumor Suppression Role for BRG 1 in Cell Cycle Control and
  • 2003
Role for BRG1 in Cell Cycle Control and Tumor Suppression
TLDR
This work provides further evidence for a role for BRG1 in the regulation of several genes involved in key steps in tumorigenesis and has revealed a potential mechanism forBRG1-induced growth arrest.
BRG-1 is required for RB-mediated cell cycle arrest.
TLDR
It is demonstrated that BRG-1 loss renders cells resistant to RB-mediated cell cycle progression, and that disruption of RB signaling through loss of cooperating factors occurs in cancer cells.
RB and hbrm cooperate to repress the activation functions of E2F1.
TLDR
It is demonstrated that the domain of hbrm that binds RB has transcriptional activation potential which RB can repress, suggesting that RB not only targets hBRm but also regulates its activity.
The Viral Oncogene Human Papillomavirus E7 Deregulates Transcriptional Silencing by Brm-related Gene 1 via Molecular Interactions*
TLDR
The results collectively suggest that the viral oncogene E7 targets both pRb and BRG-1 via protein-protein interactions, resulting in the deregulation of host cell cycle control.
Rb-mediated chromatin structure regulation and transcriptional repression
TLDR
Here, studies that address the mechanism of transcriptional repression by Rb are reviewed, particularly in the context of chromatin structure regulation.
THE MECHANISM OF RB-MEDIATED CELL CYCLE INHIBITION
TLDR
Using innovative imaging techniques, it is demonstrated that E2F sites on chromatin are the principal targets of active RB during cell cycle arrest and elucidate the critical targets and resultant phenotypes mediated by the retinoblastoma tumor suppressor protein to inhibit cellular proliferation.
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References

SHOWING 1-10 OF 65 REFERENCES
Binding of the Rb1 protein to E1A products is required for adenovirus transformation.
TLDR
The absence of both the 107kDa and 105kDa/Rb1 proteins may be involved in the development of the oncogenic phenotype of retinoblastoma cells, suggesting that E1A-mediated transformation results from the elimination of functional Rb1 protein within the cell.
The regions of the retinoblastoma protein needed for binding to adenovirus E1A or SV40 large T antigen are common sites for mutations.
TLDR
Two non‐contiguous regions of RB were found to be essential for complex formation with adenovirus E1A or SV40 large T antigen, and these results strongly suggest that these viral oncoproteins are targeting a protein domain that is an important site in the normal function of the RB protein.
BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription
TLDR
The results show that the SWI2 family DNA-dependent ATPase domain has functional con-servation between yeast and humans and suggest that a SWI/SNF protein complex is required for the activation of selective mammalian genes.
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