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E2F directly regulates the expression of late myogenic genes, with E2f1 (show E2F1 Proteins) providing the major contribution compared with E2f2.
The dE2F2 protein repress the expression of buffy, the anti-apoptotic member of the Bcl-2 (show BCL2 Proteins) family and activate the expression of an RNA-binding protein that destabilizes diap1 (show DIAPH1 Proteins) in Drosophila.
Heterozygous mutation of mip120 (show LIN54 Proteins) or E2f2 suppressed the binucleate cell phenotype in the peripodial epithelium of Myb (show MYB Proteins)-null wing discs.
dE2F2, as well as the net E2F activity, which can be depleted by mutating the common cofactor, dDp (show TIMM8A Proteins), is inhibitory for p53 (show TUBB Proteins)-independent apoptosis.
RBF1 and RBF2 interact with different subsets of E2F proteins; this enables the RBF (show ATP5I Proteins) proteins to regulate E2F-dependent transcription in distinct ways
cells containing dE2F2 require dE2F1 (show E2F1 Proteins) to either prevent, or reverse, dE2F (show E2F1 Proteins)-mediated repression
Data show that removal of p55 deregulated the expression of E2F targets that are normally repressed by dE2F2/RBF-1 and -2 complexes in a cell cycle-independent manner but had no effect on the expression of targets normally coupled with cell proliferation.
examination of linking together the Myb (show MYB Proteins) and E2F2 complexes in higher-order assembly to specific chromosomal sites for the regulation of transcription
RBF2 has a unique function in repressing E2F-regulated differentiation markers and dE2F2 and RBF2 are required to regulate different sets of target genes in different tissues
Thease results demonstrate epigenetic regulation of gene expression by Myb (show MYB Proteins), and E2F2-RBF (show ATP5I Proteins) in vivo, and also provide an explanation for the ability of Mip130-null mutants to rescue the lethality of Myb (show MYB Proteins)-null mutants in vivo.
Data indicate that microRNA miR (show MLXIP Proteins)-214 has tumor-suppressive activity in hepatocellular carcinoma (HCC (show FAM126A Proteins)) through inhibition of E2F2 transcription factor (E2F2), cyclin (show PCNA Proteins)-dependent kinases CDK3 (show CDK3 Proteins) and CDK6 (show CDK6 Proteins).
we validated for the first time that E2F2 acts as a tumor activator in non-small cell lung carcinoma.
E2F2 loss results in increased lung metastasis in breast cancer, potentially functioning through a PTPRD (show PTPRD Proteins) dependent mechanism.
Elevated E2F2 expression in glioblastoma cells weakens the effect of elevated levels of miR (show MLXIP Proteins)-218.
cell cycle-dependent transcription of the TRAIP (show TRAIP Proteins) gene by E2F1 (show E2F1 Proteins), E2F2, and E2F4 (show E2F4 Proteins) and rapid protein degradation leads to cell cycle-dependent expression with a maximum in G2/M
miR218 and miR520a are crucial in the development of hepatocellular carcinoma via the inhibition of cell proliferation and cycle progression by downregulating E2F2.
miR (show MLXIP Proteins)-31 regulated the proliferation of colon cancer cells by targeting E2F2.
Results show evidence that let-7a expression in osteosarcoma (OS) cells is significantly reduced and inversely correlated with E2F2 expression levels and that let-7a plays an important role in OS cell proliferation and tumorigenesis by targeting E2F2.
Overall, miR (show MLXIP Proteins)-155 plays an important role in colorectal carcinoma tumorigenesis by negative regulation of its targets including E2F2.
Low expression of E2F2 may reflect functional redundancy between members of the E2F (show E2F1 Proteins) family, in this case between E2F1 (show E2F1 Proteins) and E2F2.
Spinal cord injury-induced activation of E2F1 (show E2F1 Proteins)-2 mediates cell cycle activation, contributing to gliopathy and neuronal/tissue loss associated with motor impairments and post-traumatic hyperesthesia.
A role for E2F1 (show E2F1 Proteins) and E2F2 as suppressors of replicative stress in differentiating cells, and the existence of a robust E2F (show E2F1 Proteins)-p53 (show TP53 Proteins) regulatory axis in tissue homeostasis enabling and tumorigenesis preventing is shown.
E2F2 accumulates at sites of oxidative and UV-induced DNA damage, and interact with gammaH2AX (show H2AFX Proteins) DNA repair factor.
E2F2 activity sustains the hepatic homeostasis of major membrane glycerolipid components while it is dispensable for storage glycerolipid balance.
Rb-deficient cells hijack and redeploy Myc (show MYC Proteins) and E2f3 from an S-G2 (show STRN3 Proteins) program essential for normal cell cycles to a G1-S program that re-engages ectopic cell cycles, exposing an unanticipated addiction of Rb-null cells on Myc (show MYC Proteins).
showed that the D326V missense pRb (show PGR Proteins) bound to E2F1 (show E2F1 Proteins) but failed to interact with E2F2/3
E2F3 promotes while E2F2 suppresses ischemic cardiac repair through corresponding changes in endothelial cell proliferation.
E2F2 impairs, and endothelial E2F3 promotes, the angiogenic response to peripheral ischemic injury through corresponding changes in EC cell-cycle progression.
E2f2 induces cone photoreceptor apoptosis independent of E2f1 and E2f3 in mice.
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 and another 2 members, E2F1 and E2F3, have an additional cyclin binding domain. This protein binds specifically to retinoblastoma protein pRB in a cell-cycle dependent manner, and it exhibits overall 46% amino acid identity to E2F1.
, transcription factor E2F2
, E2F transcription factor 2
, hepatocyte growth factor-like protein