IndraLab

Statements

NFRKB affects UCHL5
16 | 39 29
NFRKB binds UCHL5.
16 | 18 25
UCHL5 binds NFRKB. 10 / 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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ADRM1 binds NFRKB and UCHL5. 2 / 2
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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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"Biological information indicated that both RPN13 and INO80G bind to a long fragment at the C-terminal of the UCH-L5."
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NFRKB binds UCHL5 and ULD. 1 / 1
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"In these two complexes a DEUBAD domain is present in the regulatory proteins, RPN13 and INO80G, that binds to the C-terminal ULD domain of the UCH-L5."
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NFRKB inhibits UCHL5.
| 13 4
NFRKB inhibits UCHL5. 10 / 20
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"Inhibition of UCH37 by NFRKB NTD."
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"NFRKB NTD inhibits UCH37 because of two distinct contacts that it makes with the UCH domain."
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"The related DEUBAD domain in INO80G inhibits UCH-L5 by exploiting similar structural elements in UCH-L5 to promote a radically different conformation, and employs molecular mimicry to block ubiquitin docking."
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"Mechanism of UCH-L5 Inhibition by INO80G DEU ."
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"Interestingly, UCHL5 is activated by the proteasome subunit RPN13 and inhibited by the INO80G subunit ."
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"The first example of this type is UCH-L5 inhibition by INO80G."
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"Our binding assays showed that INO80G DEU decreases the affinity of UCH-L5 for substrates (XREF_FIG A and 2B)."
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"Analysis of the UCH-L5 and INO80G DEU interface shows how the large conformational changes in UCH-L5 organize novel interfaces where key elements for ubiquitin binding and RPN13 DEU -mediated activation are exploited by INO80G DEU to inhibit UCH-L5 activity."
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"The first example of this type is UCH-L5 inhibition by INO80G."
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"For example, the inhibition of UCH-L5 by INO80G must be alleviated during DNA repair because the catalytic activity of UCH-L5 is required in this pathway [68] ."
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NFRKB activates UCHL5.
| 8
NFRKB activates UCHL5. 8 / 8
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"While the DEUBAD domain of RPN13 activates UCH-L5 by increasing its affinity for substrates, in INO80G it does the opposite and dramatically decreases the affinity for substrates."
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"To determine whether NFRKB also modulates Uch37 activity, we affinity purified from insect cells recombinant Uch37 in complexes with NFRKB, various NFRKB derivatives, or hRpn13 (XREF_SUPPLEMENTARY) and assayed Uch37 for its ability to react with ubiquitin vinylsulfone (UbVS)."
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"Why does NFRKB DEU fail to activate Uch37?"
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"Our observations are consistent with the findings that RPN13 competes with NFRKB 1-101 for binding to UCH37 and that NFRKB residues 1-101 activate UCH37 but that the longer full-length and 1-465 constructs inhibit UCH37, as do the 39-156 and 1-117 constructs used in this study."
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"Enzyme kinetics analysis confirmed that INO80G short activates UCH-L5 on Ub-AMC (XREF_FIG B)."
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"INO80G short, containing only the helices alpha2-alpha4 of the DEUBAD domain, can activate UCH-L5, demonstrating that the core DEUBAD fold is already sufficient to bind and provide modest activation."
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"Our data show how UCH-L5 activity can be modulated by DEUBAD domains present in RPN13 and INO80G through remarkably large conformational changes."
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"Intriguingly, an artificial shorter version of INO80G was found to activate UCH-L5 invitro."
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UCHL5 affects NFRKB
16 1 | 31 25
UCHL5 binds NFRKB.
16 | 18 25
UCHL5 binds NFRKB. 10 / 56
16 | 18 22
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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)."
25194926
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"Additionally, UCHL5 can also bind the DEUBAD of NFRKB, a subunit of the INO80 chromatin-remodeling complex (52, 53, 55)."
35764170
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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."
32351584
reach
"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]."
32351584
reach
"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."
32351584
reach
"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."
25702872
reach
"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
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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]."
32351584
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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."
25702870
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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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ADRM1 binds NFRKB and UCHL5. 2 / 2
| 2
sparser
"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."
18922472
sparser
"Biological information indicated that both RPN13 and INO80G bind to a long fragment at the C-terminal of the UCH-L5."
27802576
NFRKB binds UCHL5 and ULD. 1 / 1
| 1
sparser
"In these two complexes a DEUBAD domain is present in the regulatory proteins, RPN13 and INO80G, that binds to the C-terminal ULD domain of the UCH-L5."
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UCHL5 deubiquitinates NFRKB.
1 | 5
UCHL5 deubiquitinates NFRKB. 5 / 6
1 | 5
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"Combining the above results, it can be concluded that DRAIC mediates the ubiquitylation degradation of NFRKB by interfering with deubiquitination of NFRKB induced by UCHL5, and then exerts an anti-cancer effect in GC."
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"UCHL5 is also required for BLM/EXO1 dependent end resection through de-ubiquitinating the INO80 subunit NFRKB, although the function of this subunit in regulating end resection is not currently understood [37]."
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"On the other hand, Zhang et al. found that lncRNA DRAIC could suppress GC metastasis of GC cells via through influencing NFRKB de-ubiquitination induced by UCHL5 27.EMT is considered to be a core factor of tumor metastasis, and it is clear that a variety of lncRNAs participated in GC development by regulating this cell program."
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"LncRNA DRAIC inhibits proliferation and metastasis of gastric cancer cells through interfering with NFRKB deubiquitination mediated by UCHL5."
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"So we further tested the ubiquitination level of NFRKB, and found that the NFRKB ubiquitination level increased significantly after oeDRAIC, which could demonstrate that DRAIC weakens the deubiquitination of NFRKB mediated by UCHL5, and maintains the ubiquitination level of NFRKB and boost the degradation of NFRKB via the ubiquitination-proteasome pathway."
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UCHL5 inhibits NFRKB.
| 3
UCHL5 bound to NFRKB inhibits NFRKB. 2 / 2
| 2
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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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"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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UCHL5 inhibits NFRKB. 1 / 1
| 1
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"Furthermore, NFRKB reduction caused by UCHL5 depletion was rescued in cells expressing GFP-UCHL5 and was prevented by MG132 treatment (XREF_FIG and XREF_SUPPLEMENTARY)."
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UCHL5 activates NFRKB.
| 3
UCHL5 activates NFRKB. 2 / 2
| 2
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"Further studies showed that DRAIC can promote the ubiquitination degradation of NFRKB mediated by UCHL5, and confirmed the inhibitory effect of DRAIC on proliferation and metastasis of GC cells, which could be rescued by oeNFRKB."
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"UCHL5 aids resection by protecting NFRKB from proteasomal degradation."
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UCHL5 bound to NFRKB activates NFRKB. 1 / 1
| 1
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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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UCHL5 decreases the amount of NFRKB.
| 2
UCHL5 decreases the amount of NFRKB. 2 / 2
| 2
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"We found that UCHL5 depletion reduced the steady-state level of NFRKB but not hRPN13 (XREF_FIG and data not shown); and time-course studies in cells treated with cycloheximide, to prevent de novo protein synthesis, revealed that UCHL5 depletion reduced NFRKB protein half-life (XREF_FIG)."
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"UCHL5 depletion did not, however, reduce NFRKB mRNA levels, nor protein levels of other INO80-complex subunits with suggested roles in DSB repair (XREF_SUPPLEMENTARY) XREF_BIBR - XREF_BIBR."
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