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COMMD9 participates in TFDP1/E2F1 (show E2F1 Proteins) activation and plays a critical role in non-small cell lung cancer.
Here, the authors show that an acidic region of DP1 (show PTGDR Proteins), whose function has remained elusive, binds to the plekstrin homology (PH) domain of the p62 (show GTF2H1 Proteins) subunit of TFIIH (show GTF2H1 Proteins) that contributes to transcriptional activation.
role for E2F1 (show E2F1 Proteins) and TFDP1 in the transcriptional regulation of PITX1 (show PITX1 Proteins) in articular chondrocytes
According to our study results, the gene TFDP1 and the cell cycle pathway are strongly associated with high-grade glioblastoma multiforme (GBM); this result may provide new insights into the pathogenesis of GBM.
Amplification of CUL4A (show CUL4A Proteins), IRS2 (show IRS2 Proteins), and TFDP1 genes showed a significant difference in disease-free survival by both univariate and multivariate survival analyses in intrahepatic cholangiocarcinoma.
The TFDP1 indel84 mutation generates a gain-of-function phenotype by increasing cell proliferation, migration, and invasion of colorectal cancer cells.
somatic mutations in DP-1 (show PTGDR Proteins) uncouple normal control of the E2F (show E2F1 Proteins) pathway, and thus define a new mechanism that could contribute to aberrant proliferation in tumor cells
The authors demonstrate that adenovirus E1A (show BCKDHA Proteins) binds to E2F/DP (show E2F1 Proteins)-1 (show PTGDR Proteins) complexes through a direct interaction with DP-1 (show PTGDR Proteins) and may selectively activate a subset of E2F (show E2F1 Proteins)-regulated cellular genes during infection.
the DP-1 (show PTGDR Proteins) "Stabilon" domain was a C-terminal acidic motif and was quite important for DP-1 (show PTGDR Proteins) stability.
13q34 amplification may be of relevance in tumor progression of breast cancers by inducing overexpression of CUL4A (show CUL4A Proteins) and TFDP1, important in cell cycle regulation. These genes were also overexpressed in non-basal-like tumor samples.
Kbtbd5 (show KBTBD5 Proteins) regulates skeletal muscle myogenesis through the regulation of E2F1 (show E2F1 Proteins)-DP1 (show REEP5 Proteins) activity
Cell cycle suppression by Cdk5 (show CDK5 Proteins) is made through the formation of a previously unknown complex consisting of the p35 (show CDK5R1 Proteins)-Cdk5 (show CDK5 Proteins) dimer and E2F1 (show E2F1 Proteins), which excludes the E2F1 (show E2F1 Proteins) cofactor, DP1 (show REEP5 Proteins), thus inhibiting E2F1 (show E2F1 Proteins) binding to the promoters of various cell cycle genes.
Persistent PP2A (show PPP2R2B Proteins) expression prevented the appearance of the phosphorylated form of DP-1 required for cellular differentiation and reversal of dysplasia after loss of oncogene (show RAB1A Proteins) expression.
Results show that Dp1 (show REEP5 Proteins) is largely dispensable for embryonic development, despite the absolute extraembryonic requirement for Dp1 (show REEP5 Proteins).
The authors propose that these dual functions of DP1 can promote and stabilize biphasic Wnt (show WNT2 Proteins)-on and Wnt (show WNT2 Proteins)-off states in response to a gradual gradient of Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signalling to determine differential cell fates.
This gene encodes a member of a family of transcription factors that heterodimerize with E2F proteins to enhance their DNA-binding activity and promote transcription from E2F target genes. The encoded protein functions as part of this complex to control the transcriptional activity of numerous genes involved in cell cycle progression from G1 to S phase. Alternative splicing results in multiple transcript variants. Pseudogenes of this gene are found on chromosomes 1, 15, and X.
RNA-binding protein MEX3A
, transcription factor Dp-1, like
, DRTF1-polypeptide 1
, E2F dimerization partner 1
, E2F-related transcription factor
, cell cycle regulatory transcription factor DP1
, transcription factor Dp-1
, transcription factor Dp-1 a
, transcription factor Dp-1-like