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COMMD9 participates in TFDP1/E2F1 (zeige E2F1 Proteine) activation and plays a critical role in non-small cell lung cancer.
Here, the authors show that an acidic region of DP1 (zeige PTGDR Proteine), whose function has remained elusive, binds to the plekstrin homology (PH) domain of the p62 (zeige GTF2H1 Proteine) subunit of TFIIH (zeige GTF2H1 Proteine) that contributes to transcriptional activation.
role for E2F1 (zeige E2F1 Proteine) and TFDP1 in the transcriptional regulation of PITX1 (zeige PITX1 Proteine) 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 (zeige CUL4A Proteine), IRS2 (zeige IRS2 Proteine), 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 (zeige PTGDR Proteine) uncouple normal control of the E2F (zeige E2F1 Proteine) pathway, and thus define a new mechanism that could contribute to aberrant proliferation in tumor cells
The authors demonstrate that adenovirus E1A (zeige BCKDHA Proteine) binds to E2F/DP (zeige E2F1 Proteine)-1 (zeige PTGDR Proteine) complexes through a direct interaction with DP-1 (zeige PTGDR Proteine) and may selectively activate a subset of E2F (zeige E2F1 Proteine)-regulated cellular genes during infection.
the DP-1 (zeige PTGDR Proteine) "Stabilon" domain was a C-terminal acidic motif and was quite important for DP-1 (zeige PTGDR Proteine) stability.
13q34 amplification may be of relevance in tumor progression of breast cancers by inducing overexpression of CUL4A (zeige CUL4A Proteine) and TFDP1, important in cell cycle regulation. These genes were also overexpressed in non-basal-like tumor samples.
Kbtbd5 (zeige KBTBD5 Proteine) regulates skeletal muscle myogenesis through the regulation of E2F1 (zeige E2F1 Proteine)-DP1 (zeige REEP5 Proteine) activity
Cell cycle suppression by Cdk5 (zeige CDK5 Proteine) is made through the formation of a previously unknown complex consisting of the p35 (zeige CDK5R1 Proteine)-Cdk5 (zeige CDK5 Proteine) dimer and E2F1 (zeige E2F1 Proteine), which excludes the E2F1 (zeige E2F1 Proteine) cofactor, DP1 (zeige REEP5 Proteine), thus inhibiting E2F1 (zeige E2F1 Proteine) binding to the promoters of various cell cycle genes.
Persistent PP2A (zeige PPP2R2B Proteine) expression prevented the appearance of the phosphorylated form of DP-1 required for cellular differentiation and reversal of dysplasia after loss of oncogene (zeige RAB1A Proteine) expression.
Results show that Dp1 (zeige REEP5 Proteine) is largely dispensable for embryonic development, despite the absolute extraembryonic requirement for Dp1 (zeige REEP5 Proteine).
The authors propose that these dual functions of DP1 can promote and stabilize biphasic Wnt (zeige WNT2 Proteine)-on and Wnt (zeige WNT2 Proteine)-off states in response to a gradual gradient of Wnt (zeige WNT2 Proteine)/beta-catenin (zeige CTNNB1 Proteine) 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