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Cleavage stimulation factor, 3' pre-RNA, subunit 2, 64kDa

CstF-64, Cstf2
This gene encodes a nuclear protein with an RRM (RNA recognition motif) domain. The protein is a member of the cleavage stimulation factor (CSTF) complex that is involved in the 3' end cleavage and polyadenylation of pre-mRNAs. Specifically, this protein binds GU-rich elements within the 3'-untranslated region of mRNAs. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, POLYMERASE, CstF-77, CPSF, SYM
Papers on CstF-64
τCstF-64 Mediates Correct mRNA Polyadenylation and Splicing of Activator and Repressor Isoforms of the Cyclic AMP-Responsive Element Modulator (CREM) in Mouse Testis.
MacDonald et al., In Biol Reprod, Jan 2016
We found that the testis-expressed paralog of CstF-64, τCstF-64 (gene symbol Cstf2t) is involved in a polyadenylation site choice switch of Crem mRNA and leads to an overall decrease of the Crem mRNAs that are generated from internal promoters in Cstf2t(-/-) mice.
3'UTR shortening and EGF signaling: implications for breast cancer.
Erson-Bensan et al., Ankara, Turkey. In Hum Mol Genet, Jan 2016
To begin addressing the underlying mechanisms, we found CSTF2 (cleavage stimulation factor 2), a major regulator of 3'UTR shortening to be up-regulated in response to epidermal growth factor (EGF).
CstF-64 and 3'-UTR cis-element determine Star-PAP specificity for target mRNA selection by excluding PAPα.
Laishram et al., Thiruvananthapuram, India. In Nucleic Acids Res, Nov 2015
We identified a Star-PAP recognition nucleotide motif and showed that suboptimal DSE on Star-PAP target pre-mRNA 3'-UTRs inhibit CstF-64 binding, thus preventing PAPα recruitment onto it.
CstF64: cell cycle regulation and functional role in 3' end processing of replication-dependent histone mRNAs.
Schümperli et al., Bern, Switzerland. In Mol Cell Biol, 2015
The processing site is recognized by stem-loop binding protein and the U7 snRNP, but cleavage additionally requires a heat-labile factor (HLF), composed of cleavage/polyadenylation specificity factor, symplekin, and cleavage stimulation factor 64 (CstF64).
Generation of plasmid vectors expressing FLAG-tagged proteins under the regulation of human elongation factor-1α promoter using Gibson assembly.
MacDonald et al., United States. In J Vis Exp, 2014
The protocol described here is a rapid method to create plasmids expressing FLAG-tagged CstF-64 and CstF-64 mutant under the expressional regulation of the hEF1α promoter.
CstF-64 is necessary for endoderm differentiation resulting in cardiomyocyte defects.
MacDonald et al., Lubbock, United States. In Stem Cell Res, 2014
However, CstF-64 knockout (Cstf2(E6)) cells were able to differentiate into neuronal progenitors, demonstrating that some differentiation pathways were still intact.
In silico characterization of a RNA binding protein of cattle filarial parasite Setaria digitata.
Mayan et al., Colombo, Sri Lanka. In Bioinformation, 2013
The shortest ORF of 249 bp from the isolated cDNA encodes a polypeptide of 82 amino acids and shows an amino acid identity of 54% with the RRM domain of human cleavage stimulation factor-64 kDa subunit (CstF-64).
TDP-43 regulates β-adducin (Add2) transcript stability.
Muro et al., Trieste, Italy. In Rna Biol, 2013
In addition, we failed to show interaction between TDP-43 and key polyadenylation factors, such as CstF-64 and CPSF160 and excluded TDP-43 involvement in pre-mRNA cleavage and regulation of polyA tail length.
Dynamic analyses of alternative polyadenylation from RNA-seq reveal a 3'-UTR landscape across seven tumour types.
Li et al., Houston, United States. In Nat Commun, 2013
Finally, our results implicate CstF64, an essential polyadenylation factor, as a master regulator of 3'-UTR shortening across multiple tumour types.
Host factors in enterovirus 71 replication.
Li et al., Taiwan. In J Virol, 2011
The cleavage stimulation factor 64K subunit (CstF-64) is a host protein that is involved in the 3' polyadenylation of cellular pre-mRNAs, and recent work suggests that in EV71-infected cells, it may be cleaved by the EV71 3C protease.
Characterization of a cleavage stimulation factor, 3' pre-RNA, subunit 2, 64 kDa (CSTF2) as a therapeutic target for lung cancer.
Daigo et al., Tokyo, Japan. In Clin Cancer Res, 2011
CSTF2 is likely to play an important role in lung carcinogenesis and be a prognostic biomarker in the clinic.
Interactions of CstF-64, CstF-77, and symplekin: implications on localisation and function.
Schümperli et al., Bern, Switzerland. In Mol Biol Cell, 2011
nuclear accumulation of CstF-64 depends on binding to CstF-77 not symplekin; interaction between CstF-64/CstF-64Tau and CstF-77 are important for maintenance of nuclear levels of CstF complex components and intracellular localization, stability, function
The hinge domain of the cleavage stimulation factor protein CstF-64 is essential for CstF-77 interaction, nuclear localization, and polyadenylation.
MacDonald et al., Lubbock, United States. In J Biol Chem, 2010
The Hinge domain is necessary for CstF-64 interaction with CstF-77 and consequent nuclear localization.
Targeted 3' processing of antisense transcripts triggers Arabidopsis FLC chromatin silencing.
Dean et al., Norwich, United Kingdom. In Science, 2010
Through suppressor mutagenesis, we identify a requirement for CstF64 and CstF77, two conserved RNA 3'-end-processing factors, in FLC silencing.
Transcription elongation factor ELL2 directs immunoglobulin secretion in plasma cells by stimulating altered RNA processing.
Milcarek et al., Pittsburgh, United States. In Nat Immunol, 2009
ELL2 and CstF-64 tracked together with RNA polymerase II across the Igh mu- and gamma-gene segments
Characterization of Rous sarcoma virus polyadenylation site use in vitro.
McNally et al., Milwaukee, United States. In Virology, 2008
The inactivity of the RSV poly(A) site was at least in part due to poor CstF binding since tethering CstF to the RSV substrate activated polyadenylation.
Transcription and RNA processing factors play complex roles in DT40 cells.
Manley et al., New York City, United States. In Subcell Biochem, 2005
The ability to perform conditional knockouts and to generate stable transfectants in DT40 cells has facilitated the study of general transcription factors such as TATA binding proteins, essential splicing factors such as ASF/SF2 and crucial polyadenylation factors such as CstF64, as well as a number of more specific regulators of gene expression.
Alternative polyadenylation events contribute to the induction of NF-ATc in effector T cells.
Serfling et al., Würzburg, Germany. In Immunity, 1999
The relative low binding affinity of cleavage stimulation factor CstF-64 to the proximal polyA site seems to contribute to its neglect in naive T cells.
The polyadenylation factor CstF-64 regulates alternative processing of IgM heavy chain pre-mRNA during B cell differentiation.
Manley et al., New York City, United States. In Cell, 1996
Here, we show that accumulation of one subunit of an essential polyadenylation factor (CstF-64) is specifically repressed in mouse primary B cells and that overexpression of CstF-64 is sufficient to switch heavy chain expression from membrane-bound (microm) to secreted form (micros).
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