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The findings demonstrate that constitutive Tip110 expression in human cord blood CD34(+) cells is regulated, at least in part, through its interaction with CstF64, recruitment of CstF64 to, and selective usage of two polyadenylation sites within its 3'UTR.
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hnRNP H binds to two specific G-runs in exon 5a of ACHE and activates the distal alternative 3 splice site (ss) between exons 5a and 5b. Furthermore, hnRNP H competes for binding of CstF64 to the overlapping binding sites in exon 5a, and suppresses the selection of a cryptic polyadenylation site, which additionally ensures transcription of the distal 3 ss required for the generation of AChET isoform.
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CstF-64 is dispensable for the expression/3'-end processing of Star-PAP target mRNAs.CstF-64 and 3'-UTR cis-element determine Star-PAP specificity for target mRNA selection by excluding poly A polymerase.
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CstF64, an essential polyadenylation factor, is a master regulator of 3'-UTR shortening across multiple tumour types.
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CstF64 is central to the function of a heat-labile factor, composed of cleavage/polyadenylation specificity factor, symplekin, and cleavage stimulation factor 64 and appears to be at least partly responsible for its cell cycle regulation.
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CstF64 and CstF64tau modulate one another's expression and play overlapping as well as distinct roles in regulating global alternative polyadenylation profiles.
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CstF64 binds to thousands of dormant intronic PASs that are suppressed, at least in part, by U1 small nuclear ribonucleoproteins
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CSTF2 is likely to play an important role in lung carcinogenesis and be a prognostic biomarker in the clinic.
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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
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The Hinge domain is necessary for CstF-64 interaction with CstF-77 and consequent nuclear localization.
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dynamics of the CstF-64 RNA-binding domain, both free and bound to two GU-rich RNA sequences that represent polyadenylation regulatory elements, by NMR Spectroscopy
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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.
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CstF64 (cstf2) and not other CstF subunits induced by lipopolysaccharide (LPS) in murine macrophages and changes polyA site use
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Describes the induction of CSTF2 in the growth phase of cells.
