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UCHL5 binds NFRKB. 40 / 56
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"Interestingly, immunoprecipitation studies from MG132 treated cells revealed that NFRKB interacted with UCHL5 less in the chromatin fraction than in the nucleoplasm, despite its interactions with INO80 being essentially equivalent in these two fractions (XREF_FIG; for input fractions, see XREF_SUPPLEMENTARY)."
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"Additionally, UCHL5 can also bind the DEUBAD of NFRKB, a subunit of the INO80 chromatin-remodeling complex (52, 53, 55)."
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"DRAIC combined with UCHL5 and attenuated binding of UCHL5 and NFRKB, meanwhile promoting the degradation of NFRKB via ubiquitination, and then inhibited the proliferation and metastasis of GC cells, which can be rescued by oeNFRKB."
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"Similarly, the results of bioinformatics analysis and Co-IP assay demonstrated that UCHL5 interacted with NFRKB, which is consistent with the research by Sahtoe DD et al. [XREF_BIBR]."
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"However, the effect of DRAIC on the combination of UCHL5 and NFRKB was still unclarified, so we detected this combination in oeDRAIC and shDRAIC cell lines, whose results showed that oeDRAIC can significantly reduce the level of NFRKB coprecipitated by UCHL5, while shDRAIC can increase NFRKB binding with UCHL5, which confirmed the speculation that DRAIC may indirectly down-regulate the expression of NFRKB through affecting the deubiquitination induced by UCHL5."
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"Recruitment to INO80 is mediated by the N-terminal domain of NFRKB (NFRKB NTD), which also binds the UCH37 CTD and, in sharp contrast to RPN13, further inhibits UCH37 activity."
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"Considering the deubiquitination function of UCHL5, we speculated that DRAIC might regulate the ubiquitination level of NFRKB by influencing the binding of UCHL5 and NFRKB, and then affect the protein expression of NFRKB."
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"At the same time, Co-IP assay confirmed the interaction between UCHL5 and NFRKB, which is in accord with the research by Nishi R [XREF_BIBR]."
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"On the other hand, INO80G DEU binds to UCH-L5 and uses ULD conformational flexibility to dock its unique inhibitory FRF hairpin into the Leu38 pocket."
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"The activity of UCH-L5 is enhanced when UCH-L5 combines with proteasome 19S regulatory subunit by Rpn13 and Admr1 receptor and inhibited when UCH-L5 interacts with NFRKB."
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"And UCH-L5 also interacts with NFRKB in INO80 complex, but it remains unknown that whether UCH-L5 interacts with other components of INO80 complex or not."
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"The activity of UCH-L5 is enhanced when UCH-L5 combines with proteasome 19S regulatory subunit by Rpn13/Admr1 receptor and inhibited when UCH-L5 interacts with NFRKB."
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"Importantly, two-hybrid assays detected an interaction between NFRKB and full-length Uch37, but not a truncated Uch37 that retains only the UCH domain."
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"While the activity of UCH-L5 is inhibited when UCH-L5 interacts with NFRKB, a component of INO80 complex, by combination and deubiquitination [ xref ]."
29371935
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"And UCH-L5 also interacts with NFRKB in INO80 complex, but it remains unknown that whether UCH-L5 interacts with other components of INO80 complex or not."
29371935
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"Additionally, UCHL5 can also bind the DEUBAD of NFRKB, a subunit of the INO80 chromatin-remodeling complex ( xref , xref , xref )."
35764170
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"DRAIC is down-regulated in GC tissues and cell lines while its potential interacting molecules UCHL5 and NFRKB are up-regulated, and DRAIC is positively correlated with NFRKB protein instead of mRNA."
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"The authors found that UCH-L5 interacted with and stabilized NFRKB."
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"DRAIC combined with UCHL5 and attenuated binding of UCHL5 and NFRKB, meanwhile promoting the degradation of NFRKB via ubiquitination, and then inhibited the proliferation and metastasis of GC cells, which can be rescued by oeNFRKB."
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"Confirming the importance of the N-terminal 101 residues for stable association between Uch37 and NFRKB, Flag-NFRKB co-immunoprecipitated with endogenous Uch37 from HEK293 cells, whereas NFRKBDeltaN101, which lacked the first 101 amino acids, failed to do so (XREF_FIG)."
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"Nevertheless, the N101 fragment appears to account only partially for NFRKB binding to Uch37."
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"Unexpectedly, however, both the longer N465 fragment and full-length NFRKB blocked formation of the Uch37-UbVS adduct."
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"The above bioinformatics results suggested that DRAIC, UCHL5 and NFRKB may interact with each other and exert biological effects in GC."
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"Nevertheless, the N101 fragment appears to account only partially for NFRKB binding to Uch37."
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"To define in more detail the interaction between Uch37 and NFRKB, we generated a series of fragments from the N-terminal third of NFRKB by in vitro translation using a bacterial cell-free system and tested their abilities to interact with GST-Uch37 in GST-pulldown assays."
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"Previous work has established that UCHL5 is a component of both the proteasome and the INO80 chromatin remodeling complex; these complexes being mediated via UCHL5 interactions with hRPN13 and NFRKB ( n uclear f actor r elated to κ B- b inding protein), respectively ( xref ) xref , xref , xref ."
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"In gastric cancer, DRAIC combined with UCHL5 to attenuate the binding of UCHL5 and NFRKB, thereby promoting the degradation of NFRKB via ubiquitination and inhibiting the proliferation and metastasis [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Because hRpn13 and NFRKB interact with Uch37 in the proteasome and hINO80, respectively, we asked whether the isolated proteins bind to Uch37 in a mutually exclusive fashion."
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"The association of Uch37 with the DNA-binding NFRKB subunit of INO80 suggests that Uch37’s role in gene regulation could be restricted to specific genes that contain NFRKB binding sites."
18922460
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"Similarly, the results of bioinformatics analysis (Fig.  xref a bottom) and Co-IP assay (Fig.  xref c) demonstrated that UCHL5 interacted with NFRKB, which is consistent with the research by Sahtoe DD et al. [ xref ]."
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"UCHL5 interacts with and protects NFRKB (also known as INO80G) that is a component of INO80 chromatin remodeling complex from proteasomal degradation by removing K48 linked ubiquitin chain."
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"Interestingly, immunoprecipitation studies from MG132-treated cells revealed that NFRKB interacted with UCHL5 less in the chromatin fraction than in the nucleoplasm, despite its interactions with INO80 being essentially equivalent in these two fractions ( xref ; for input fractions, see xref )."
25194926
sparser
"However, the effect of DRAIC on the combination of UCHL5 and NFRKB was still unclarified, so we detected this combination in oeDRAIC and shDRAIC cell lines, whose results showed that oeDRAIC can significantly reduce the level of NFRKB coprecipitated by UCHL5 (Fig.  xref d), while shDRAIC can increase NFRKB binding with UCHL5 (Fig.  xref e), which confirmed the speculation that DRAIC may indirectly down-regulate the expression of NFRKB through affecting the deubiquitination induced by UCHL5."
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"UCHL5 is another subunit in the INO80 complex, it has been shown that NFRKB interacts with the C-terminal of UCHL5 through the DEUBAD domain to inhibiting the deubiquitase activity of UCHL5 [17] ."
35093437
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"Preliminary research found that NFRKB bind to the C-terminus of UCHL5 through the N-terminal domain (residues 1–476) [17] ."
35093437
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"Briefly, the DEUBAD domain of NFRKB can interact with UCHL5, in which the main role is played by the FRF hairpin and helix α6 ( Fig. 2 )."
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"Moreover, ubiquitin vinyl sulfone ( UbVS ) is a probe that it can detect the deubiquitinating activity, both NFRKB 1-465 fragment and full-length NFRKB blocked the formation of UCHL5-UbVS adduct, whic[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
35093437
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"Considering the deubiquitination function of UCHL5, we speculated that DRAIC might regulate the ubiquitination level of NFRKB by influencing the binding of UCHL5 and NFRKB, and then affect the protein expression of NFRKB."
32351584
sparser
"At the same time, Co-IP assay confirmed the interaction between UCHL5 and NFRKB, which is in accord with the research by Nishi R [ xref ]."
32351584
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"In gastric cancer, DRAIC combined with UCHL5 to attenuate the binding of UCHL5 and NFRKB, thereby promoting the degradation of NFRKB via ubiquitination and inhibiting the proliferation and metastasis [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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