showed that inhibiting the SLBP mRNA and protein levels were rescued by epigenetic modifiers suggesting that nickel's effects on SLBP may be mediated via epigenetic mechanisms
CRL4(WDR23) is required for efficient histone mRNA 3' end processing to produce mature histone mRNAs for translation. CRL4(WDR23) binds and ubiquitylates SLBP in vitro and in vivo and this modification activates SLBP function in histone mRNA 3' end processing without affecting its protein levels.
arsenic a carcinogenic metal decreases cellular levels of SLBP by inducing its proteasomal degradation and inhibiting SLBP transcription via epigenetic mechanisms
the S/G2 stable mutant form of SLBP is degraded by proteasome in G1 indicating that indicating that the SLBP degradation in G1 is independent of the previously identified SLBP degradation at S/G2
Alternative splicing allows the synthesis of HBP/SLBP isoforms with different properties that may be important for regulating HBP/SLBP functions during replication stress.
Data suggest that oligomerization and SLBP phosphorylation regulate SLBP-SLIP1-histone-mRNA complex formation/disassociation; sequential and ordered assembly is required; This paper describes the biophysical characterization of human SLBP and the SLBP-SLIP1 complex. Human SLBP is an intrinsically disordered protein that is phosphorylated at 23 Ser/Thr sites when expressed in a eukaryotic expression system such as baculovirus. Unphosphorylated human SLBP forms a high affinity heterotetramer with SLIP1 and the SLBP-SLIP1 complex is regulated by SLBP phosphorylation.
Using yeast two-hybrid screening the authors identify CT initiation factor-interacting protein (CTIF) as a protein that binds directly to SLBP. SLBP preferentially associates with the CT complex of histone mRNAs consisting of CBP80/CBP20 but not with the eIF4E/eIF4G (ET) complex as has been proposed. Rapid degradation of histone mRNA on the inhibition of DNA replication requires association of SLBP with CTIF.
This paper shows that SLBP is a substrate for the prolyl isomerase Pin1. Pin1 along with PP2A facilitates dissociation of the SLBP-histone mRNA complex at the end of S-phase thereby promoting histone mRNA decay and SLBP ubiquitination.
The nuclear magnetic resonance and kinetic studies presented here provide a framework for understanding how SLBP recognizes histone mRNA and highlight possible structural roles of phosphorylation and proline isomerization in RNA binding proteins
Here we show that NELF interacts with the cap binding complex (CBC) a factor that plays important roles in mRNA processing steps and the two factors together participate in the 3' end processing of histone mRNAs through association with the SLBP.
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