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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Cleavage and polyadenylation specific factor 3, 73kDa

CPSF, CPSF-73
Most eukaryotic mRNA precursors (pre-mRNAs) undergo extensive maturational processing, including cleavage and polyadenylation at the 3-prime end. CPSF3 encodes the 73-kD subunit of the cleavage and polyadenylation specificity factor (CPSF) and is the pre-mRNA 3-prime-end-processing endonuclease (Mandel et al., 2006 [PubMed 17128255]).[supplied by OMIM, Jul 2010] (from NCBI)
Top mentioned proteins: POLYMERASE, CAN, Histone, SYM, PAP
Papers on CPSF
The polyadenylation complex of Trypanosoma brucei: characterization of the functional poly(A) polymerase.
New
Preußer et al., Gießen, Germany. In Rna Biol, Feb 2016
Based on tandem-affinity purification with tagged CPSF160 and mass spectrometry, we identified ten associated components of the trypanosome polyadenylation complex, including homologues to all four CPSF subunits, Fip1, CstF50/6;4, and Symplekin, as well as two hypothetical proteins.
Global analysis of CPSF2-mediated alternative splicing: Integration of global iCLIP and transcriptome profiling data.
New
Green et al., United States. In Genom Data, Dec 2015
Using a genome-wide RNA interference screening strategy, we identified cleavage and polyadenylation specificity factor (CPSF) and symplekin (SYMPK) as cofactors of the well-known splicing regulator RBFOX2.
Universal RNA-degrading enzymes in Archaea: Prevalence, activities and functions of β-CASP ribonucleases.
Review
New
Quentin et al., Toulouse, France. In Biochimie, Nov 2015
Three β-CASP orthologous groups, aCPSF1, aCPSF2, aCPSF1b, are closely related to the eukaryal CPSF73 termination factor and one, aRNase J, is ortholog of the bacterial RNase J.
The Y3** ncRNA promotes the 3' end processing of histone mRNAs.
New
Hüttelmaier et al., Halle, Germany. In Genes Dev, Nov 2015
We demonstrate that the Y3/Y3** noncoding RNAs (ncRNAs) bind to the CPSF (cleavage and polyadenylation specificity factor) and that Y3** associates with the 3' untranslated region (UTR) of histone pre-mRNAs.
A Biogenesis Step Upstream of Microprocessor Controls miR-17∼92 Expression.
New
Impact
Gregory et al., Boston, United States. In Cell, Sep 2015
The endonuclease CPSF3 (CPSF73) and the spliceosome-associated ISY1 are responsible for pro-miRNA biogenesis and expression of all miRNAs within the cluster except miR-92.
In vivo characterization of the Drosophila mRNA 3' end processing core cleavage complex.
New
Steiniger et al., Saint Louis, United States. In Rna, Aug 2015
A core cleavage complex (CCC) consisting of CPSF73, CPSF100, and Symplekin is required for cotranscriptional 3' end processing of all metazoan pre-mRNAs, yet little is known about the in vivo molecular interactions within this complex.
Global Promotion of Alternative Internal Exon Usage by mRNA 3' End Formation Factors.
New
Green et al., Worcester, United States. In Mol Cell, Jul 2015
Unexpectedly, we find that two mRNA 3' end formation factors, cleavage and polyadenylation specificity factor (CPSF) and SYMPK, are RBFOX2 cofactors for both inclusion and exclusion of internal exons.
CPSF30 at the Interface of Alternative Polyadenylation and Cellular Signaling in Plants.
Review
Hunt et al., Lexington, United States. In Biomolecules, 2014
A considerable amount of research has been done in characterizing different subunits of so-called Cleavage and Polyadenylation Specificity Factor (CPSF).
Emergence of the β-CASP ribonucleases: highly conserved and ubiquitous metallo-enzymes involved in messenger RNA maturation and degradation.
Review
Clouet-d'Orval et al., Chapel Hill, United States. In Biochim Biophys Acta, 2013
Recent phylogenomic analyses have shown that the β-CASP ribonucleases can be partitioned into two major subdivisions that correspond to orthologs of eukaryal CPSF73 and bacterial RNase J.
Few Smad proteins and many Smad-interacting proteins yield multiple functions and action modes in TGFβ/BMP signaling in vivo.
Review
Huylebroeck et al., Leuven, Belgium. In Cytokine Growth Factor Rev, 2011
In this survey, we selected appropriate examples on the BMP-Smads, with emphasis on Smad1 and Smad5, and on a number of SIPs, i.e. the CPSF subunit Smicl, Ttrap (Tdp2) and Sip1 (Zeb2, Zfhx1b) from our own research carried out in three different vertebrate models.
An active role for splicing in 3'-end formation.
Review
Martinson, Los Angeles, United States. In Wiley Interdiscip Rev Rna, 2011
Finally, the U2 snRNP interacts with CPSF in a step resembling spliceosomal A-complex formation.
The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA.
GeneRIF
Anderson et al., Madison, United States. In Embo J, 2011
The data support a model where Star-PAP binds to the pre-mRNA, recruits the CPSF complex to the 3'-end of pre-mRNA and then defines cleavage by CPSF 73 and subsequent polyadenylation of its target mRNAs.
The tumor suppressor Cdc73 functionally associates with CPSF and CstF 3' mRNA processing factors.
GeneRIF
Meyerson et al., Boston, United States. In Proc Natl Acad Sci U S A, 2009
The tumor suppressor Cdc73 functionally associates with CPSF and CstF 3' mRNA processing factors.
CSR1 induces cell death through inactivation of CPSF3.
GeneRIF
Luo et al., Pittsburgh, United States. In Oncogene, 2009
CSR1 appears to induce cell death through a novel mechanism by hijacking a critical RNA processing enzyme CPSF3.
Studies of the 5' exonuclease and endonuclease activities of CPSF-73 in histone pre-mRNA processing.
GeneRIF
Dominski et al., Chapel Hill, United States. In Mol Cell Biol, 2009
Degradation of the downstream cleavage product (DCP) does not depend on the Xrn2 5' exonuclease, suggesting that CPSF-73 degrades the DCP both in vitro and in vivo.
Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3'-end maturation.
GeneRIF
Steitz et al., New Haven, United States. In Embo Rep, 2008
Conserved residues in CPSF2 and CPSF-73 are required for assembly of the endonuclease activity that cleaves histone pre-mRNAs.
Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease.
Impact
GeneRIF
Tong et al., New York City, United States. In Nature, 2007
crystal structures of human CPSF-73 at 2.1 A resolution, complexed with zinc ions and a sulphate that might mimic the phosphate group of the substrate; CPSF-73 is the pre-mRNA 3'-end-processing endonuclease
Integrator, a multiprotein mediator of small nuclear RNA processing, associates with the C-terminal repeat of RNA polymerase II.
Impact
Shiekhattar et al., Philadelphia, United States. In Cell, 2005
Two of the Integrator subunits display similarities to the subunits of the cleavage and polyadenylation specificity factor (CPSF) complex.
The polyadenylation factor CPSF-73 is involved in histone-pre-mRNA processing.
Impact
Marzluff et al., Chapel Hill, United States. In Cell, 2005
Immunoprecipitation experiments identified this protein as CPSF-73, a known component of the cleavage/polyadenylation machinery.
Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic polyadenylation.
Impact
Richter et al., Worcester, United States. In Cell, 2004
In Xenopus oocytes, where the molecular mechanism has been defined, the core factors that control this process include CPEB, an RNA binding protein whose association with the CPE specifies which mRNAs undergo polyadenylation; CPSF, a multifactor complex that interacts with the near-ubiquitous polyadenylation hexanucleotide AAUAAA; and maskin, a CPEB and eIF4E binding protein whose regulation of initiation is governed by poly(A) tail length.
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