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SART3 binds USP15. 88 / 94
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"However, Tip110 was found to interact with and promote nuclear translocation of USP4 and USP15 but not USP11, and this is due to β-hairpin of the linker region of the DUSP and UBL domains of both USP4 and USP15 proteins that were associated with the HAT domain of Tip110 (12, 23, 25, 38) In addition, the binding of USP15 to Tip110 is 20-fold stronger than USP4 (55)."
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"Those observations prompted us to investigate whether Tip110-USP15 complex regulate NF-κB activity."
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"On the other hand, okadaic acid did not show any significant effect on the USP15 and SART3 interaction ( Fig. 4 c)."
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"In addition, the NLS of SART3 binds importin-α in a bipartite manner, and SART3 interaction with USP4 and USP15 induces translocation of USP4 and USP15 into the nucleus [12] ."
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"We further show that SART3 is associated with the ubiquitin-specific peptidase USP15 and that ZNNT1 may induce p53 destabilization by inhibiting this interaction."
37448957
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"These results suggest that ZNNT1 interferes with the SART3-USP15 complex-mediated stabilization of p53 protein and thereby plays important roles in the proliferation and tumorigenicity of colon cancer cells."
37448957
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"We further show that SART3 is associated with the ubiquitin-specific peptidase USP15 and that ZNNT1 induces p53 destabilization by inhibiting the interaction between p53 and the SART3-USP15 complex."
37448957
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"We further show that ZNNT1 promotes proteasomal degradation of p53 by interfering with the interaction between p53 and the SART3-USP15 complex."
37448957
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"Moreover, Co-IP results showed that depleting either USP15 or BARD1 did not impair the association of SART3 with BRAD1 or USP15 (Supplementary Fig.  xref )."
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"ZNNT1 interferes with the SART3-USP15 complex-mediated stabilization of p53."
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"Pull-down assays using either anti-SART3 or anti-USP15 antibody confirmed the association of SART3 with USP15 in HCT116 cells (Fig. xref A)."
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"These results suggest that ZNNT1 interacts with the SART3-USP15 complex and interferes with its binding to p53, and thereby induces p53 degradation (Fig. xref E)."
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"Consistent with this notion, we found that SART3 is associated with the deubiquitinase USP15 in colon cancer cells."
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"Thus, ZNNT1 may inhibit the interaction between the SART3-USP15 complex and p53, and thereby induces p53 degradation and cell proliferation."
37448957
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"However, it remains to be elucidated how the SART3-USP15 complex affects p53 ubiquitination by MDM2 and other ubiquitin ligases."
37448957
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"We further showed that ZNNT1 induces p53 degradation by interfering with the interaction between p53 and the SART3-USP15 complex (Fig. xref D)."
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"USP15 interacts with SART3."
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"Therefore, the interaction between SART3 and USP15 in the cells was examined."
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"We next examined whether SART3 forms a complex with USP15 and USP4 simultaneously using sequential immunoprecipitation."
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"As shown in xref , SART3 interacted with USP15 1–226 but not with USP15 230–952 ."
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"Taken together, these data show that USP15 interacts with SART3 directly through the DUSP-UBL domains."
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"Furthermore, Tip110 interacts with USP15 and regulates its localization between the cytoplasm and nucleus ( xref , xref ), while USP15 is shown to regulate NF-κB activity ( xref , xref , xref )."
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"These findings suggest that the SART3-USP15 cascade disruption could result in chronic ER stress, which would speed up the neurodegenerative phenotype [ xref ]."
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"USP15 interacts with SART3."
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"Therefore, the interaction between SART3 and USP15 in the cells was examined."
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"As shown in XREF_SUPPLEMENTARY, SART3 interacted with USP15 1-226 but not with USP15 230-952."
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"However, Tip110 was found to interact with and promote nuclear translocation of USP4 and USP15 but not USP11, and this is due to β-hairpin of the linker region of the DUSP and UBL domains of both USP4 and USP15 proteins that were associated with the HAT domain of Tip110 ( xref , xref , xref , xref ) In addition, the binding of USP15 to Tip110 is 20-fold stronger than USP4 ( xref )."
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"Those observations prompted us to investigate whether Tip110-USP15 complex regulate NF-κB activity."
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"USP15 and USP4 form a complex with SART3."
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"Therefore, SART3 predominantly binds to USP15, and this complex may exhibit a higher preference for binding to TUT1 compared to USP4 alone.Next, we examined whether USP4 deubiquitinates TUT1."
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"These findings suggest SART3 binds to both USP15 and USP4, and this may lead to deubiquitination of PRP31 and PRP3 simultaneously."
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"Therefore, SART3 predominantly binds to USP15, and this complex may exhibit a higher preference for binding to TUT1 compared to USP4 alone."
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"As discussed above, USP15 interacts with SART3, a factor known to increase the deubiquitinating activity of USP15 [ xref ]."
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"To determine the specificity of Tip110 interaction with USP15, we took advantage of the approximate N- and C-terminal domain deletion mutants of these two proteins and performed the similar immunoprec[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The U4/U6 recycling factor SART3 has histone chaperone activity and associates with USP15 to regulate H2B deubiquitination."
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"In agreement with our findings, one recent study shows that USP15 binds to Tip110 and regulates histone 2b deubiquitination ( Long et al., 2014 )."
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"Because USP15 bound to and deubiquitinated Tip110 protein, we reasoned that USP15 could affect the stability of hTip110 in the transgenic mice."
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"Moreover, it was reported that Sart3, Usp4 and Usp15 form a complex in order to de-ubiquitinate Prp3 and Prp31 simultaneously."
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"Moreover, as a substrate recruiting factor of USP15 either, SART3 can simultaneously bind USP4 and USP15, serving as a platform to deubiquitinate PRP31 and PRP3."
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"As seen in Fig. 3 a and b, the interaction between SART3 and USP15 phosphomimetics decreased with respect to the corresponding phosphomutants."
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"They demonstrated that Tip110 also interacts with USP15 and affects its nuclear localization."
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"To examine whether a synergistic effect of the two phosphorylations exists in modulating the USP15 and SART3 interaction, both the Thr149 and Thr219 phosphorylation sites of USP15 were mutated."
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"The observations of the altered interactions between SART3 and the phosphorylated USP15 at positions T149 and T219 prompted us to analyze the deubiquitinating activity toward PRP31 in the spliceosome."
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"Furthermore, the purvalanol A treatment increased the interaction of USP15 with SART3 ( Fig. 4 c)."
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"On the other hand, okadaic acid did not show any significant effect on the USP15 and SART3 interaction ( Fig. 4 c)."
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"Taken together, these results indicate that both N and C termini of USP15 but only N terminus of Tip110 are involved in complex formation between Tip110 and USP15 and provide the indirect evidence for[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Thus, it is conceivable that complex formation between Tip110 and USP15 contributes to regulation of Tip110 degradation through USP15-mediated deubiquitination."
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"In agreement with our findings, one recent study shows that USP15 binds to Tip110 and regulates histone 2b deubiquitination ( Long et al., 2014 )."
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"In addition, the other study reports that USP4, the USP15 homolog, binds to Tip110 and deubiquitinates Prp3, component of the U4 snRNP, during the spilceosome cycle ( Song et al., 2010 )."
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"Thus, it is most likely that an unknown E3 ligase enzyme exists within Tip110/USP15 complex and has not been identified with our proteomic study due to the transient nature of their interaction.The di[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"But, unfortunately, the two sites are not defined in the crystal structure of the SART3–USP15 DUSP-UBL complex reported earlier [13] ."
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"LncRNA ZNNT1 induces p53 degradation by interfering with the interaction between p53 and the SART3-USP15 complex."
37448957
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"These results suggest that ZNNT1 interferes with the SART3-USP15 complex-mediated stabilization of p53 protein and thereby plays important roles in the proliferation and tumorigenicity of colon cancer cells."
37448957
reach
"We further show that SART3 is associated with the ubiquitin-specific peptidase USP15 and that ZNNT1 induces p53 destabilization by inhibiting the interaction between p53 and the SART3-USP15 complex."
37448957
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"Thus, ZNNT1 may inhibit the interaction between the SART3-USP15 complex and p53, and thereby induces p53 degradation and cell proliferation."
37448957
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"We further show that ZNNT1 promotes proteasomal degradation of p53 by interfering with the interaction between p53 and the SART3-USP15 complex."
37448957
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"ZNNT1 interferes with the SART3-USP15 complex-mediated stabilization of p53."
37448957
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"These results suggest that ZNNT1 interacts with the SART3-USP15 complex and interferes with its binding to p53, and thereby induces p53 degradation (Fig. 5E)."
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"However, it remains to be elucidated how the SART3-USP15 complex affects p53 ubiquitination by MDM2 and other ubiquitin ligases.In our previous study, we established cell lines with different tumorigenicity and performed RNA-seq analysis to identify lncRNA UPAT, which plays a critical role in the proliferation and tumorigenicity of colon cancer cells."
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"We further showed that ZNNT1 induces p53 degradation by interfering with the interaction between p53 and the SART3-USP15 complex (Fig. 5D)."
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"Our finding demonstrated that ABHD11-AS1 directly and specifically binds to SART3; (ii) Previous studies reported that SART3 interacts with deubiquitinase USP15 and promotes USP15 nuclear localization to regulate RNA alternative splicing."
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"Previous reports have revealed that SART3 interacts with deubiquinase USP15 (Ubiquitin-Specific Peptidase 15) and promotes its nuclear localization to regulate RNA alternative splicing ( xref ; xref )."
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"These findings, On the other hand, could not rule out the possibility that ABHD11-AS1 may promote USP15 nuclear localization by modifying either SART3 or USP15 to increase SART3-USP15 interaction through undefined mechanisms."
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"The binding between SART3 and USP15 was validated through co-IP ( Fig. 5 a)."
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"Indeed, USP15 specifically binds to SART3 (also known as Tip110) via DUSP domain and removes ubiquitin from both SART3 and its binding partner, histone H2B XREF_BIBR XREF_BIBR XREF_BIBR."
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