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Cleavage and polyadenylation specific factor 6

The protein encoded by this gene is one subunit of a cleavage factor required for 3' RNA cleavage and polyadenylation processing. The interaction of the protein with the RNA is one of the earliest steps in the assembly of the 3' end processing complex and facilitates the recruitment of other processing factors. The cleavage factor complex is composed of four polypeptides. This gene encodes the 68kD subunit. It has a domain organization reminiscent of spliceosomal proteins. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, TRN-SR2, Nup153, ACID, Peptidylprolyl Isomerase
Papers on CPSF6
HIV-1 Capsid Stabilization Assay.
Diaz-Griffero et al., United States. In Methods Mol Biol, Dec 2015
We also found that purified CPSF6 (1-321) protein stabilizes in vitro-assembled HIV-1 CA-NC complexes (Fricke et al., J Virol 87:10587-10597, 2013).
Fusion of PDGFRB to MPRIP, CPSF6, and GOLGB1 in three patients with eosinophilia-associated myeloproliferative neoplasms.
Fabarius et al., Mannheim, Germany. In Genes Chromosomes Cancer, Dec 2015
We here report the identification of three new PDGFRB fusion genes in three male MPN-eo patients: MPRIP-PDGFRB in a case with t(5;17)(q33;p11), CPSF6-PDGFRB in a case with t(5;12)(q33;q15), and GOLGB1-PDGFRB in a case with t(3;5)(q13;q33).
Direct Visualization of HIV-1 Replication Intermediates Shows that Capsid and CPSF6 Modulate HIV-1 Intra-nuclear Invasion and Integration.
Brass et al., Worcester, United States. In Cell Rep, Dec 2015
Direct visualization of HIV-1 replication would improve our understanding of the viral life cycle.
HIV-1 Resistance to the Capsid-Targeting Inhibitor PF74 Results in Altered Dependence on Host Factors Required for Virus Nuclear Entry.
Aiken et al., Nashville, United States. In J Virol, Sep 2015
The mutant capsid structure was not significantly perturbed by binding of PF74; rather, the mutations inhibited capsid interactions with CPSF6 and Nup153 and altered HIV-1 dependence on these host factors and on TNPO3.
Functional label-free assays for characterizing the in vitro mechanism of action of small molecule modulators of capsid assembly.
Pagratis et al., Foster City, United States. In Biochemistry, May 2015
We also used these assays to characterize the interaction between capsid and the host protein cleavage and polyadenylation specific factor 6 (CPSF6).
Compensatory substitutions in the HIV-1 capsid reduce the fitness cost associated with resistance to a capsid-targeting small-molecule inhibitor.
Aiken et al., Nashville, United States. In J Virol, 2015
5Mut substitutions also reduced the binding of the host protein CPSF6 to assembled CA complexes in vitro and permitted infection of cells expressing the inhibitory protein CPSF6-358.
Whole transcriptome sequencing reveals extensive unspliced mRNA in metastatic castration-resistant prostate cancer.
Li et al., Houston, United States. In Mol Cancer Res, 2015
Using quantitative PCR (qPCR), a series of genes (AR, KLK2, KLK3, STEAP2, CPSF6, and CDK19) were confirmed to have a greater proportion of unspliced RNA in CRPC specimens than in normal prostate epithelium, untreated primary prostate cancer, and cultured prostate cancer cells.
Structural basis of HIV-1 capsid recognition by PF74 and CPSF6.
Yeager et al., Charlottesville, United States. In Proc Natl Acad Sci U S A, 2015
Here we report biochemical experiments showing that PF-3450074 (PF74), a drug that inhibits HIV-1 infection, as well as host proteins cleavage and polyadenylation specific factor 6 (CPSF6) and nucleoporin 153 kDa (NUP153), bind to the CA hexamer with at least 10-fold higher affinities compared with nonassembled CA or isolated CA domains.
Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly.
James et al., Cambridge, United Kingdom. In Plos Pathog, 2014
Here we show that a multi-subunit interface formed exclusively within CA hexamers mediates binding to linear epitopes within cellular cofactors NUP153 and CPSF6, and is competed for by the antiretroviral compounds PF74 and BI-2.
Impairment of HIV-1 cDNA synthesis by DBR1 knockdown.
Camerini et al., Irvine, United States. In J Virol, 2014
When nuclear import of the HIV-1 reverse transcription complex was blocked by expressing a truncated form of the mRNA cleavage and polyadenylation factor CPSF6, the completion of HIV-1 vector cDNA synthesis was detected in the cytoplasm, where it was not inhibited by DBR1 knockdown.
A model for cofactor use during HIV-1 reverse transcription and nuclear entry.
Towers et al., London, United Kingdom. In Curr Opin Virol, 2014
We present a model that may explain how the capsid protein has a fundamental role in the early part of the viral lifecycle by utilising cyclophilin A (CypA), cleavage and polyadenylation specificity factor-6 (CPSF6), Nup358 and TNPO3 to orchestrate a coordinated process of DNA synthesis, capsid uncoating and integration targeting that evades innate responses and promotes integration into preferred areas of chromatin.
Decipher the dynamic coordination between enzymatic activity and structural modulation at focal adhesions in living cells.
Wang et al., San Diego, United States. In Sci Rep, 2013
Utilizing biosensors based on fluorescence resonance energy transfer (FRET), we developed a correlative FRET imaging microscopy (CFIM) approach to quantitatively analyze the subcellular coordination between the enzymatic Src activation and the structural FA disassembly.
BI-2 destabilizes HIV-1 cores during infection and Prevents Binding of CPSF6 to the HIV-1 Capsid.
Diaz-Griffero et al., United States. In Retrovirology, 2013
FINDINGS: This work demonstrates that BI-2 destabilizes the HIV-1 core during infection, and prevents the binding of the cellular factor CPSF6 to the HIV-1 core.
Quantitative microscopy of functional HIV post-entry complexes reveals association of replication with the viral capsid.
Kräusslich et al., Heidelberg, Germany. In Elife, 2013
We further show that the CA-targeted inhibitor PF74 exhibits a bimodal mechanism, blocking RTC/PIC association with the host factor CPSF6 and nuclear entry at low, and abrogating reverse transcription at high concentrations.
HIV-1 evades innate immune recognition through specific cofactor recruitment.
Towers et al., London, United Kingdom. In Nature, 2013
Here we show that HIV-1 capsid mutants N74D and P90A, which are impaired for interaction with cofactors cleavage and polyadenylation specificity factor subunit 6 (CPSF6) and cyclophilins (Nup358 and CypA), respectively, cannot replicate in primary human monocyte-derived macrophages because they trigger innate sensors leading to nuclear translocation of NF-κB and IRF3, the production of soluble type 1 IFN and induction of an antiviral state.
HIV-1 capsid-targeting domain of cleavage and polyadenylation specificity factor 6.
Kewalramani et al., Frederick, United States. In J Virol, 2012
A 9-residue stretch of hydrophobic amino acids in CPSF6 restricts HIV-1 infection through an interaction with capsid.
Structural basis of pre-mRNA recognition by the human cleavage factor Im complex.
Teng et al., Hefei, China. In Cell Res, 2011
The study reports the crystal structure of human cleavage factor I(m), comprising cleavage factor I(m)25 and the RNA recognition motif domain of cleavage factor I(m)68 kDa (CF I(m)68RRM).
Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping.
Doublié et al., Burlington, United States. In Structure, 2011
Structure of a CFI(m)25/CFI(m)68 RRM heterotetramer and biochemical data indicated that CFIm25 specifically recognized two UGUA elements, CFIm68 facilitates looping of the intervening RNA. CFIm-mediated RNA looping may regulate alternative polyadenylation
Evidence that cleavage factor Im is a heterotetrameric protein complex controlling alternative polyadenylation.
Yamaguchi et al., Yokohama, Japan. In Genes Cells, 2010
Data provide evidence that CFIm exists as a heterotetramer of 25-kD, 59-kD and 68-kD subunits of CFIm: CFIm25, CFIm59 and CFIm68.
Flexible use of nuclear import pathways by HIV-1.
KewalRamani et al., Frederick, United States. In Cell Host Microbe, 2010
HIV-1 harboring the N74D mutation in capsid protein fails to interact with CPSF6 and evades the nuclear import restriction.
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