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Overexpression of PD2 leads to increased tumorigenicity and metastasis in pancreatic ductal adenocarcinoma.
Propose that degradation of MYC (show MYC Proteins) limits the accumulation of MYC (show MYC Proteins)/PAF1C complexes during transcriptional activation.
Mechanistic studies indicated that PAF1C could promote lung cancer cell proliferation through regulating c-MYC (show MYC Proteins) transcription.
CNOT4 (show CNOT4 Proteins) controls the degradation of chromatin-unbound PAF1 (show PEX2 Proteins) via the 26S proteasome (show Psmd4 Proteins).
this study found that Pol II-associated factor 1 (PAF1 (show PEX2 Proteins)) is a critical regulator of paused Pol II release, that positive transcription elongation factor b (P-TEFb (show CDK9 Proteins)) directly regulates the initial recruitment of PAF1 (show PEX2 Proteins) complex (PAF1C) to genes, and that the subsequent recruitment of CDK12 (show CRKRS Proteins) is dependent on PAF1C.
This study reveals an evolutionarily conserved role for PAF1 (show PEX2 Proteins) as a regulator of promoter-proximal pausing by RNA Pol II in all metazoans, including human.
PD2 is a novel cancer stem cell (CSC) maintenance protein, loss of which renders the CSCs more susceptible to drug-induced cell death.
Together, these results indicate that human adenovirus E1A (show BCKDHA Proteins) uses hBre1 (show RNF20 Proteins) to recruit the hPaf1 complex in order to optimally activate viral early transcription by enhancing transcriptional elongation.
The results show that the Paf1 (show PEX2 Proteins)/Leo1 (show LEO1 Proteins) heterodimer is necessary for its binding to histone H3 (show HIST3H3 Proteins), the histone octamer, and nucleosome in vitro.
E1A (show BCKDHA Proteins) changes the function of hBre1 (show RNF20 Proteins) from a ubiquitin ligase involved in substrate selection to a scaffold which recruits hPaf1 as a means to stimulate transcription and transcription-coupled histone modifications.
link Paf1C with PolII elongation and RNA processing indicates that Paf1C subunits could play roles in controlling transcript length through suppression of PolII accumulation at transcription start site (TSS (show RPL38 Proteins))-proximal pA sites
The PAF1 (show PEX2 Proteins) complex is required for mammalian development, likely through regulation of H3K36me3, indicating a functional conservation of the PAF1 (show PEX2 Proteins) complex from yeast to mammals in vivo.
As part of a cell-intrinsic transcriptional pathway, Paf1 (show PEX2 Proteins) regulates neuronal migration in the brain.
MLL (show MLL Proteins) interacts directly with the polymerase associated factor complex (PAFc) via Paf1 (show PEX2 Proteins) and CTR9. PAFc augments MLL (show MLL Proteins) and MLL (show MLL Proteins)-AF9 (show MLLT3 Proteins) mediated transcriptional activation of Hoxa9 (show HOXA9 Proteins) and their interaction is essential for leukemogenesis.
show that Paf1/PD2 is overexpressed in mouse embryonic stem cells (ESCs (show NR2E3 Proteins)) and is involved in the maintenance of mouse ESCs (show NR2E3 Proteins).
The PAF1 complex differentially regulates cardiomyocyte specification.
This gene encodes a subunit of the polymerase associated factor (PAF1) complex. The PAF1 complex interacts with RNA polymerase II and plays a role in transcription elongation as well as histone modifications including ubiquitylation and methylation. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
RNA polymerase II-associated factor 1 homolog
, pancreatic differentiation protein 2
, PD2-like protein
, paf1, RNA polymerase II associated factor, homolog, like