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Literature DB >> 15075294

TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel pRb-independent and E2F1-specific control for cell survival.

Kang Liu¹, Yuhong Luo, Fang-Tsyr Lin, Weei-Chin Lin.

Abstract

TopBP1 (DNA topoisomerase IIbeta binding protein I) contains multiple BRCT domains and is involved in replication and the DNA damage checkpoint. Through its BRCT domain, TopBP1 interacts with and represses exclusively E2F1 but not other E2F factors. This regulation of E2F1 transcriptional activity is mediated by a pRb-independent, but Brg1/Brm-dependent mechanism. TopBP1 recruits Brg1/Brm, a central component of the SWI/SNF chromatin-remodeling complex, to E2F1-responsive promoters and represses the activities of E2F1, but not E2F2 or E2F3. This regulation is crucial in the control of E2F1-dependent apoptosis during normal cell growth and DNA damage. Interestingly, TopBP1 is induced by E2F and interacts with E2F1 during G1/S transition. Thus, TopBP1 functions as a critical modulator and serves as a negative feedback regulator of E2F1 by inhibiting E2F1-dependent apoptosis during G1/S transition as well as DNA damage to promote cell survival.

Entities: Gene

Mesh：

Substances：

Year: 2004 PMID： 15075294 PMCID： PMC387242 DOI： 10.1101/gad.1180204

Source DB: PubMed Journal: Genes Dev ISSN： 0890-9369 Impact factor: 11.361

55 in total

1. Analysis of promoter binding by the E2F and pRB families in vivo: distinct E2F proteins mediate activation and repression.

Authors: Y Takahashi; J B Rayman; B D Dynlacht
Journal: Genes Dev Date: 2000-04-01 Impact factor: 11.361

Review 2. The Rb/E2F pathway: expanding roles and emerging paradigms.

Authors: J W Harbour; D C Dean
Journal: Genes Dev Date: 2000-10-01 Impact factor: 11.361

3. Cut5 is required for the binding of Atr and DNA polymerase alpha to genotoxin-damaged chromatin.

Authors: Edgardo R Parrilla-Castellar; Larry M Karnitz
Journal: J Biol Chem Date: 2003-10-02 Impact factor: 5.157

4. Identification of a protein-binding site in the promoter of the human thymidine kinase gene required for the G1-S-regulated transcription.

Authors: Y K Kim; A S Lee
Journal: J Biol Chem Date: 1992-02-05 Impact factor: 5.157

TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel pRb-independent and E2F1-specific control for cell survival.

1. Analysis of promoter binding by the E2F and pRB families in vivo: distinct E2F proteins mediate activation and repression.

Review 2. The Rb/E2F pathway: expanding roles and emerging paradigms.

3. Cut5 is required for the binding of Atr and DNA polymerase alpha to genotoxin-damaged chromatin.

4. Identification of a protein-binding site in the promoter of the human thymidine kinase gene required for the G1-S-regulated transcription.

Review 5. Chromatin as an essential part of the transcriptional mechanism.

6. A role for E2F1 in the induction of ARF, p53, and apoptosis during thymic negative selection.

7. BRG-1 is required for RB-mediated cell cycle arrest.

8. Role for the p53 homologue p73 in E2F-1-induced apoptosis.

9. A common E2F-1 and p73 pathway mediates cell death induced by TCR activation.

10. The BRCT domain is a phospho-protein binding domain.

1. TopBP1 mediates mutant p53 gain of function through NF-Y and p63/p73.

2. DNA damage signals through differentially modified E2F1 molecules to induce apoptosis.

3. E2F1 localizes to sites of UV-induced DNA damage to enhance nucleotide excision repair.

4. Dampened activity of E2F1-DP and Myb-MuvB transcription factors in Drosophila endocycling cells.

Review 5. The E2F family: specific functions and overlapping interests.

6. A role for 14-3-3 tau in E2F1 stabilization and DNA damage-induced apoptosis.

7. Claspin operates downstream of TopBP1 to direct ATR signaling towards Chk1 activation.

8. TopBP1 contains a transcriptional activation domain suppressed by two adjacent BRCT domains.

9. Mutant p53 perturbs DNA replication checkpoint control through TopBP1 and Treslin.

10. MCPH1/BRIT1 cooperates with E2F1 in the activation of checkpoint, DNA repair and apoptosis.