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CPSF6-capsid interactions allow the virus to bypass peripheral heterochromatin and penetrate the nuclear structure for integration.
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The authors demonstrate that CFIm functions as an enhancer-dependent activator of mRNA 3' processing. CFIm regulates global alternative polyadenylation by specifically binding and activating enhancer-containing poly(A) sites.
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High CPSF6 expression is associated with HIV infections.
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we found CPSF6 and all core paraspeckles proteins to be overexpressed in human breast cancer cases and their expression to correlate with poor patient outcomes.
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Studies suggest that binding of cleavage factor Im (CFIm) may be one of the earliest steps in promoting formation of an active cleavage complex.
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CPSF6 binding to its docking site in HIV-1 capsid leads to the recruitment of CFIm tetramer, suggesting that CFIm mediates CPSF6 function(s) in integration site targeting.
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integration targeting proceeds via two distinct mechanisms: capsid-CPSF6 binding directs HIV-1 to actively transcribed euchromatin, where the integrase-LEDGF/p75 interaction drives integration into gene bodies.
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NUP153 and CPSF6 have overlapping binding sites, but each makes unique capsid monomers (CA) interactions. Multiple ligands share an overlapping interface in HIV-1 capsid that is lost upon viral disassembly.
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Structural basis of HIV-1 capsid recognition by PF74 and CPSF6.
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study uncovers two opposing CA-dependent functions of CPSF6 in HIV-1 replication in vivo; however, the benefit for binding CPSF6 appears to outweigh the cost, providing support for a vital function of CPSF6 during HIV-1 replication in vivo
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CPSF6 binds specifically to a novel proteinprotein interface on the N-terminal domain of HIV-1 capsid protein (CA).
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These results suggested that inhibition of HIV-1 by TNPO3-depleted cells requires CPSF6.
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Loss-of-function of CFIm68 and CFIm25 leads to a transcriptome-wide increase in the use of proximal polyadenylation sites in HEK293 cells.
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TNPO3 promotes HIV-1 infectivity indirectly, by shifting the CA-binding protein CPSF6 to the nucleus, thus preventing the excessive HIV-1 CA stability that would otherwise result from cytoplasmic accumulation of CPSF6.
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A carboxy-terminally truncated human CPSF6 lacking residues encoded by exon 6 inhibits HIV-1 cDNA synthesis and promotes capsid disassembly.
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Knockdown of CF I(m)68 induced a systematic use of proximal polyadenylation sites, indicating that changes in relative abundance of a single 3' end processing factor can modulate the length of 3' untranslated regions across the transcriptome.
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A 9-residue stretch of hydrophobic amino acids in CPSF6 restricts HIV-1 infection through an interaction with capsid.
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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).
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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
