Current understanding of CREPT and p15RS, carboxy-terminal domain (CTD)-interacting proteins, in human cancers

  title={Current understanding of CREPT and p15RS, carboxy-terminal domain (CTD)-interacting proteins, in human cancers},
  author={Mengdi Li and Danhui Ma and Zhijie Chang},
  pages={705 - 716}
CREPT and p15RS, also named RPRD1B and RPRD1A, are RPRD (regulation of nuclear pre-mRNA-domain-containing) proteins containing C-terminal domain (CTD)-interacting domain (CID), which mediates the binding to the CTD of Rpb1, the largest subunit of RNA polymerase II (RNAPII). CREPT and p15RS are highly conserved, with a common yeast orthologue Rtt103. Intriguingly, human CREPT and p15RS possess opposite functions in the regulation of cell proliferation and tumorigenesis. While p15RS inhibits cell… Expand

Figures from this paper

RPRD Proteins Control Transcription in Human Cells
The data indicate that RPRD2 exerts the most substantial impact on transcription and has the potential to alter key biological processes including the cellular stress response and cell growth. Expand
CREPT is required for murine stem cell maintenance during intestinal regeneration
CREPT is identified as maintaining murine intestinal stem cells, with embryonic deletion causing impaired cell proliferation and regeneration, and CREPT deficiency downregulates Wnt signaling by impairing β-catenin accumulation in the nucleus of the crypt cells during regeneration. Expand


Structural basis for the recognition of RNA polymerase II C-terminal domain by CREPT and p15RS
It is proposed that dimerization through the C-terminal domain enhances the binding strength between CREPT or p15RS with Pol II by increasing binding avidity. Expand
RPRD1A and RPRD1B Are Human RNA Polymerase II C-Terminal Domain Scaffolds for Ser5 Dephosphorylation
It is shown here that RPRD1A and R PRD1B form homodimer and heterodimers through their coiled-coil domains and interact preferentially via CTD-interaction domains (CIDs) with RNAPII CTD repeats phosphorylated at S2 and S7. Expand
CREPT/RPRD1B, a Recently Identified Novel Protein Highly Expressed in Tumors, Enhances the β-Catenin·TCF4 Transcriptional Activity in Response to Wnt Signaling*
The study suggests that CREPT acts as an activator to promote transcriptional activity of the β-catenin·TCF4 complex in response to Wnt signaling, which results in up-regulated cell proliferation and invasion. Expand
p15RS/RPRD1A (p15INK4b-related Sequence/Regulation of Nuclear Pre-mRNA Domain-containing Protein 1A) Interacts with HDAC2 in Inhibition of the Wnt/β-Catenin Signaling Pathway*
Background: p15RS/RPRD1A inhibits Wnt/β-catenin signaling by recruiting HDAC2. Results: p15RS interacts with HDAC2 and enhances the occupancy of HDAC2 to promoters of Wnt-targeted genes, keepingExpand
Identification and characterization of P15RS, a novel P15(INK4b) related gene on G1/S progression.
Sequence analysis revealed that P15RS cDNA encoded a 312-amino-acid peptide containing a RAR domain that is involved in regulation of nuclear pre-mRNA, which suggests that P 15RS may be a nuclear regulation protein. Expand
The Kub5-Hera/RPRD1B interactome: a novel role in preserving genetic stability by regulating DNA mismatch repair
This work used tandem affinity purification-mass spectrometry, co-immunoprecipitation and gel-filtration chromatography to define higher-order protein complexes containing K-H scaffolding protein to gain insight into its cellular functions and discovered several novel associated proteins that function in RNA metabolism, DNA repair/replication processes and in protein metabolic processes, including translation. Expand
CREPT and p15RS regulate cell proliferation and cycling in chicken DF‐1 cells through the Wnt/β‐catenin pathway
CREPT and p15RS regulate cell proliferation and the cell‐cycle transition in chicken DF‐1 cells by regulating the transcription of Wnt/β‐catenin pathway downstream regulatory genes. Expand
Control of the RNA polymerase II phosphorylation state in promoter regions by CTD interaction domain-containing proteins RPRD1A and RPRD1B
Three previously uncharacterized human CTD-interaction domain (CID)-containing proteins, RPRD1A, R PRD1B and RPRd2, are identified by affinity purification and mass spectrometry, which co-purify with RNAP II and three otherRNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. Expand
Ser7 Phosphorylation of the CTD Recruits the RPAP2 Ser5 Phosphatase to snRNA Genes
Results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5. Expand
A Nuclear Matrix Protein Interacts with the Phosphorylated C-Terminal Domain of RNA Polymerase II
It is shown that the CTD-interacting domain of SCAF8 specifically binds CTD molecules phosphorylated on serines 2 and 5 of the consensus sequence Tyr1Ser2Pro3Thr4Ser5Pro6Ser7, which indicates a possible role forSCAF8 in linking transcription and pre-mRNA processing. Expand