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CSTF2  -  cleavage stimulation factor, 3' pre-RNA,...

Homo sapiens

Synonyms: CF-1 64 kDa subunit, CSTF 64 kDa subunit, Cleavage stimulation factor 64 kDa subunit, Cleavage stimulation factor subunit 2, CstF-64
 
 
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Disease relevance of CSTF2

  • The first 60 nucleotides of the major element have 68% identity to the negative regulatory element of HPV-16, and these elements bind the same cellular proteins, CstF-64, U2AF(65), and HuR [1].
 

High impact information on CSTF2

  • Using a yeast two-hybrid screen to identify factors that interact with the polyadenylation factor CstF-64, we uncovered an interaction with the transcriptional coactivator PC4 [2].
  • To extend this observation, we disrupted the endogenous CstF-64 gene in the B cell line DT40 and replaced it with a regulatable transgene [3].
  • Strikingly, a 10-fold decrease in CstF-64 concentration did not markedly affect cell growth but specifically and dramatically reduced accumulation of IgM heavy chain mRNA [3].
  • CstF 64 kDa and CPSF 100 kDa were distributed in a fibrogranular pattern in the nucleoplasm and, in addition, were concentrated in 1-4 bright foci [4].
  • In CstF-64, a small region, highly conserved in metazoa, is responsible for interactions with two proteins, CstF-77 and symplekin, a nuclear protein of previously unknown function [5].
 

Biological context of CSTF2

 

Anatomical context of CSTF2

  • The RNA 3' cleavage factors CstF 64 kDa and CPSF 100 kDa are concentrated in nuclear domains closely associated with coiled bodies and newly synthesized RNA [4].
  • The concentration of one CstF subunit (CstF-64) increases during activation of B cells, and this is sufficient to switch IgM heavy chain mRNA expression from membrane-bound form to secreted form [3].
 

Associations of CSTF2 with chemical compounds

  • A striking effect on nuclear structures was observed with latrunculin B, an inhibitor of actin polymerization, resulting in the formation of needlelike nuclear spicules made up of CstF-64, CPSF-100, RNA, and RNA polymerase II [7].
  • Changing Pro-41 to a serine residue in the CstF-64 RBD did not affect its affinity for poly(U)(18), but changes in amino acids downstream of the C-terminal alpha-helical region decreased affinity towards poly(U)(18) [8].
 

Physical interactions of CSTF2

  • Coimmunoprecipitation analysis indicates that a proportion of CstF-64 protein resides in the same complex as DDX1 [6].
  • HSF1 also complexes in a stress-induced manner with the 3' processing factor CstF-64 [9].
 

Regulatory relationships of CSTF2

 

Other interactions of CSTF2

  • However, CstF-64 had a higher affinity for poly(U)(18) than tauCstF-64, whereas it had a lower affinity for poly(GU)(9) [8].
  • Moreover, HCMV infection of HFFs increased the abundance of the PA cleavage stimulatory factor CstF-64, the potent splicing suppressor PTB, and the hypophosphorylated form of the splicing factor SF2 at 4 h postinfection [11].
  • Moreover, the protein was found to localize in 1-6 subnuclear domains where PML and CstF64 proteins were also identified [12].
  • Two IFN-alpha-inducible proteins, soluble N-ethylmaleimide-sensitive factor attachment protein alpha (alpha-SNAP) and cleavage stimulation factor-64 (CstF-64) previously not described in this context, were identified [10].

References

  1. The human papillomavirus type 31 late 3' untranslated region contains a complex bipartite negative regulatory element. Cumming, S.A., Repellin, C.E., McPhillips, M., Radford, J.C., Clements, J.B., Graham, S.V. J. Virol. (2002) [Pubmed]
  2. Evolutionarily conserved interaction between CstF-64 and PC4 links transcription, polyadenylation, and termination. Calvo, O., Manley, J.L. Mol. Cell (2001) [Pubmed]
  3. Levels of polyadenylation factor CstF-64 control IgM heavy chain mRNA accumulation and other events associated with B cell differentiation. Takagaki, Y., Manley, J.L. Mol. Cell (1998) [Pubmed]
  4. The RNA 3' cleavage factors CstF 64 kDa and CPSF 100 kDa are concentrated in nuclear domains closely associated with coiled bodies and newly synthesized RNA. Schul, W., Groenhout, B., Koberna, K., Takagaki, Y., Jenny, A., Manders, E.M., Raska, I., van Driel, R., de Jong, L. EMBO J. (1996) [Pubmed]
  5. Complex protein interactions within the human polyadenylation machinery identify a novel component. Takagaki, Y., Manley, J.L. Mol. Cell. Biol. (2000) [Pubmed]
  6. Association of human DEAD box protein DDX1 with a cleavage stimulation factor involved in 3'-end processing of pre-MRNA. Bléoo, S., Sun, X., Hendzel, M.J., Rowe, J.M., Packer, M., Godbout, R. Mol. Biol. Cell (2001) [Pubmed]
  7. Dynamic nature of cleavage bodies and their spatial relationship to DDX1 bodies, Cajal bodies, and gems. Li, L., Roy, K., Katyal, S., Sun, X., Bléoo, S., Godbout, R. Mol. Biol. Cell (2006) [Pubmed]
  8. Polyadenylation proteins CstF-64 and tauCstF-64 exhibit differential binding affinities for RNA polymers. Monarez, R.R., Macdonald, C.C., Dass, B. Biochem. J. (2007) [Pubmed]
  9. HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin. Xing, H., Mayhew, C.N., Cullen, K.E., Park-Sarge, O.K., Sarge, K.D. J. Biol. Chem. (2004) [Pubmed]
  10. Proteomic and transcriptomic characterization of interferon-alpha-induced human primary T helper cells. Rosengren, A.T., Nyman, T.A., Syyrakki, S., Matikainen, S., Lahesmaa, R. Proteomics (2005) [Pubmed]
  11. Convergence of RNA cis elements and cellular polyadenylation factors in the regulation of human cytomegalovirus UL37 exon 1 unspliced RNA production. Su, Y., Adair, R., Davis, C.N., DiFronzo, N.L., Colberg-Poley, A.M. J. Virol. (2003) [Pubmed]
  12. Prothymosin alpha is localized in mitotic spindle during mitosis. Vareli, K., Frangou-Lazaridis, M. Biol. Cell (2004) [Pubmed]
 
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