LASTR promotes splicing efficiency by controlling SART3 association with the U4 and U6 small nuclear ribonucleoproteins (snRNP) during spliceosome recycling.
In vitro binding experiments revealed that the RNA-recognition motifs within the SART3 sequence are responsible for selective pre-miR-34a binding. Our results provide evidence for a significant role of SART3 in miR-34a biogenesis and cell cycle progression in non-small-cell lung cancer (NSCLC) cells.
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.
Data suggest that ZIP USP39 Prp24/p100/SART3 and Prp43 associate to form complex instrumental in spliceosome assembly; ZIP regulates pre-mRNA splicing of USP39 independent of RNA binding; stable 35S tri-snRNP particles are enriched in Cajal body. (ZIP = zinc finger and G-patch domain-containing protein; USP39 = ubiquitin specific peptidase 39; Prp43 = RNA helicase Prp43)
We show that PRP31 a component of U4 snRNP is modified with K63-linked ubiquitin chains by the PRP19 complex and deubiquitinated by USP15 and its substrate targeting factor SART3. USP15SART3 makes a complex with USP4 and this ternary complex serves as a platform to deubiquitinate PRP31 and PRP3
crystal structures of SART3 in the apo-form and in complex with the DUSP-UBL domain of USP15 at 2.0 and 3.0 A respectively. Structural analysis reveals SART3 contains 12 half-a-tetratricopeptide (HAT) repeats organized into two subdomains HAT-N and HAT-C. SART3 dimerizes through the concave surface of HAT-C whereas the HAT-C convex surface binds USP15 in a novel bipartite mode.
The complex structure of SART3 nuclear localization signal (NLS) and importin-alpha reveals bipartite binding and removal of SART3 NLS prevents the entry of USP4 (and USP15) into the nucleus and abrogates the subsequent deubiquitinase activity of USP4.
Hypoxia led to Tip110 protein degradation through the ubiquitin-proteasome system. Under hypoxia Tip110 stabilized p53 which in return destabilized Tip110.
findings show C-MYC upregulates transcription of TIP110 through interaction with the TIP110 E-box in the TIP110 promoter ensuring high-level Tip110 expression in proliferating embryonic stem cells (hESCs); further show TIP110 regulates OCT4 alternative splicing in hESCs
Both purified and recombinant LSm2-8 proteins are able to recruit p110 protein to U6 snRNA via interaction with the highly conserved C-terminal region of p110.
Tip110 is a negative regulator of AR transcriptional activation and may be directly involved in AR-related developmental physiological and pathological processes
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