anti-Cleavage and Polyadenylation Specific Factor 6, 68kDa (CPSF6) Antikörper

Mouse (Murine) Cleavage and Polyadenylation Specific Factor 6, 68kDa (CPSF6) Interaktionspartner

1. Here we report that the CFIm subunits NUDT21/CPSF5 and CPSF6 are highly enriched in mouse male germ cells relative to somatic cells.

Human Cleavage and Polyadenylation Specific Factor 6, 68kDa (CPSF6) Interaktionspartner

1. The crystal structure of the RSLD-TNPO3 complex revealed potential CPSF6 interaction residues, which were confirmed to mediate TNPO3 binding and CPSF6 nuclear import. Both binding and nuclear import were independent of RSLD phosphorylation, though a hyperphosphorylated mimetic mutant failed to bind TNPO3 and mislocalized to the cell cytoplasm

2. Study shows that the cellular alternative RNA processing factor CPSF6 plays an important role in the ability of NP1 to suppress internal polyadenylation at (pA)p, in influencing viral mRNA export, and, thus, in modulating gene expression of minute virus of canines, a parvovirus.The cellular RNA processing factor CPSF6 interacted with NP1 in transfected cells and participated with NP1 to modulate its effects.

3. A novel CPSF6-RARG fusion transcript in acute myeloid leukemia.

4. CPSF6-capsid interactions allow the virus to bypass peripheral heterochromatin and penetrate the nuclear structure for integration.

5. 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.

6. High CPSF6 expression is associated with HIV infections.

7. 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.

8. Studies suggest that binding of cleavage factor Im (CFIm) may be one of the earliest steps in promoting formation of an active cleavage complex.

9. 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.

10. 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.

11. 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.

12. Structural basis of HIV-1 capsid recognition by PF74 and CPSF6.

13. 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

14. CPSF6 binds specifically to a novel proteinprotein interface on the N-terminal domain of HIV-1 capsid protein (CA).

15. These results suggested that inhibition of HIV-1 by TNPO3-depleted cells requires CPSF6.

16. Loss-of-function of CFIm68 and CFIm25 leads to a transcriptome-wide increase in the use of proximal polyadenylation sites in HEK293 cells.

17. 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.

18. A carboxy-terminally truncated human CPSF6 lacking residues encoded by exon 6 inhibits HIV-1 cDNA synthesis and promotes capsid disassembly.

19. 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.

20. A 9-residue stretch of hydrophobic amino acids in CPSF6 restricts HIV-1 infection through an interaction with capsid.