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HSP27 promotes cell cycle progression of MRC-5 cells by suppressing expression of the transcriptional repressors E2F-4 and p130
E2f4 forms apical cytoplasmic organizing centres for assembly and nucleation of deuterosomes. Using genetically altered mice and E2F4 mutant proteins we demonstrate that centriole amplification is crucially dependent on these organizing centres and that, without cytoplasmic E2f4, deuterosomes are not assembled, halting multiciliogenesis
Studied expression of E2F4 in breast cancer patients undergoing neoadjuvant chemotherapy; found target gene-based signature of E2F4 can be used to predict neoadjuvant response.
The authors found that phosphorylation of residues S650 and S975 in p107 weakens the E2F4 transactivation domain binding.
E2F4 gene expression in glioblastoma.
Integrative genomic analyses confirm that E2F4 or E2F1 expression level is high in liposarcoma patients which associate with unfavorable prognosis.
This study found evidence that the number of triplet AGC repeats in the E2F4 gene may play a role in the susceptibility to early-onset colorectal cancer.
PHF8 reduces the H3K9me2 level at the E2F4 transcriptional start site, demonstrating a direct function of PHF8 in endothelial E2F4 gene regulation
cell cycle-dependent transcription of the TRAIP gene by E2F1, E2F2, and E2F4 and rapid protein degradation leads to cell cycle-dependent expression with a maximum in G2/M
Authors show that BRCA1 and RAD17 genes, whose derived proteins play a pivotal role in DNA damage repair, are transcriptional targets of gain-of-function mutant p53 proteins.
Data suggest that aberrant cell cycle activation in Ewing sarcoma is due to the de-repression of transcription factor E2F targets of transcriptional induction and physical recruitment of E2F3 by fusion protein EWS-FLI1 replacing E2F4 on their promoters.
The inverse immunohistochemical relationship between E2F1 and E2F4 indicates a possible mechanistic interlink in colorectal cancer.
E2F4 promoter occupancy is globally associated with p53-repression targets, but not with p53 activation targets.
cancer-associated E2F4 mutations enhance the capacity of colorectal cancer cells to grow without anchorage, thereby contributing to tumor progression.
Analysis data from a panel of cell cycle transcription factors (E2F1, E2F4, E2F6, and GABPA) finds that a set of core cell cycle genes regulated in both U2OS and HeLa cells are bound by multiple cell cycle transcription factors.
Short alleles (<13 repeats) of (AGC)n in E2F4 were less frequent in women with breast cancer than in the control sample.
the loss of CDH1/E2F4 may be associated with worse clinical and pathological findings in mammary ductal carcinoma.
Trim28 regulates cell proliferation by bridging HDAC1 and E2F3 and E2F4 interactions.
In terminally differentiated cells, common KDM5A and E2F4 gene targets were bound by the pRB-related protein p130, a DREAM complex component.
Silica could induce the high expression of cyclin D1 and CDK4 and the low expression of E2F-4, resulting in the cell cycle changes by AP-1/cyclin D1 pathway in human embryonic lung fibroblasts.
E2f4 and E2f5 display overlapping roles in controlling the normal development of the male reproductive system.
Following stress exposure, E2F4-p130 complexes are lost rapidly along with the presence of E2F4 at E2F-containing B-Myb promoter sites.
E2F4 is part of a transcriptional repressor complex comprising p130 and HDAC1 in cardiac myocytes. Relief from E2F4-dependent gene silencing induces the expression of pro-apoptotic genes.
We report here a new cellular function of p27 as a transcriptional regulator in association with p130/E2F4 complexes that could be relevant for tumorigenesis.
Induction of Wnt/beta-catenin signaling in mouse mesenchymal stem cells is associated with activation of the p130 and E2f4 and formation of the p130/Gsk3beta/beta-catenin complex.
E2F4 plays an important role in enabling osteoblast progenitors to exit the cell cycle and subsequently differentiate thereby contributing to the commitment of these cells to the bone lineage.
Our data indicate that E2F4 is required for cardiomyocyte proliferation and suggest a function for E2F4 in mitosis
E2F4 controls cell cycle exit through different mechanisms.
interactions are regulated by G1 cyclin/cyclin-dependent kinase-coordinated phosphorylation of endogenous pocket proteins
E2F4 has a role in adipogenesis independent of its cell cycle regulatory activity
E2F3a and E2F4, but not E2F5, function to induce cell cycle entry, although E2F4 has more modest activity. E2F3a may induce cell death primarily through activation of p73alpha.
macrocytic anemia of E2f4(-/-) mice results primarily from impaired cellular proliferation and that the major role of E2f4 in fetal erythropoiesis is to promote cell cycle progression and cellular proliferation.
Required to determine the appropriate development of the airway epithelium.
This study investigated if the distribution between nucleus and cytoplasm of the transcription factors E2F4 and E2F5 is mediated by pRb2/p130 and if the presence of JCV T-antigen may impair this shuttling by sequestering pRb2/p130.
A novel requirement is established for cell cycle regulatory protein E2F4 in the development of the ventral telencephalon.
The E2F transcription factors are key cell cycle regulators that play important roles in modulating cell proliferation and cell fate.
normal growth-arrested enterocytes contain p130-E2F4 complexes and T-antigen expression of SV40 destroys these complexes
Cell cycle genes are the evolutionarily conserved targets of the E2F4 transcription factor
The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein binds to all three of the tumor suppressor proteins pRB, p107 and p130, but with higher affinity to the last two. It plays an important role in the suppression of proliferation-associated genes, and its gene mutation and increased expression may be associated with human cancer.
, transcription factor E2F4
, E2F transcription factor 4, p107/p130-binding
, E2F transcription factor 4