IndraLab

Statements


37 4 | 42 94

sparser
"We thus used AlphaFold2 to predict the association of UCHL5 with ADRM1."

sparser
"On mammalian proteasomes, Rpn13 binds the DUB Uch37 (refs. xref – xref ), which is not present in S. cerevisiae ."

sparser
"However, while the interaction of UCH37 with Adrm1 activates the hydrolysis of the in vitro substrate Ub-AMC, it does not activate the hydrolysis of diubiquitin xref ."

sparser
"From these data, we conclude that KDT-11 does not antagonize Rpn13-Rpn2 nor Rpn13-Uch37 binding."

sparser
"Uch37 binds through Adrm1, a previously unrecognized orthologue of Saccharomyces cerevisiae Rpn13p, which in turn is bound to the S1 (also known as Rpn2) subunit of the 19S complex."

sparser
"As expected, hRpn13 (253-407) binds Uch37 and intermolecular NOE interactions ( xref ) defined a compact binding surface composed of residues from H2, the H2-H3 loop, and H9 ( xref )."

sparser
"This suggests that a specific interaction between UCH37 and ADRM1 occurs and we can hypothesise that this role of TsUCH37, releasing Ub from proteins targeted for degradation, has been conserved throughout evolution."

sparser
"Alanine substitutions of Val286, Asp287, Glu295, and Ile296 or of Lys371, Asp373, Glu375, and Lys379 reduces ( xref , Lane 2) or abrogates ( xref , lane 4) hRpn13 binding to Uch37."

sparser
"The consolidated structure of the 26S proteasome has shown that UCH-L5 associates with the Rpn13 subunit of the 19S lid complex of the proteasome ( xref )."

sparser
"Additionally, there has been recent development of another competitive FP assay that includes fluorescently-labeled monoubiquitin bound to the Uch37:Rpn13 complex and then competed off with unlabeled ubiquitin chains."

sparser
"Previous studies have shown that hRpn2 activates ADRM1 by binding directly to ADRM1 and that activated ADRM1 interacts with the deubiquitinase UCH37 and then exerts its deubiquitination effect [ xref ]."

sparser
"As shown in Fig.  xref a and b, pro-SFTPB negatively regulated the binding of hRpn2 and UCH37 to ADRM1."

sparser
"The ubiquitin C-terminal hydrolase Uch37 (also called UCHL5) associates with the ubiquitin receptor Rpn13 and likely functions in cleaving or editing distal ubiquitin chains on proteasome substrates ( xref – xref )."

sparser
"The proteolytic activity requires a Ub receptor called ADRM1 (named hRpn13 in humans) binding to UCH37 via its C-terminal 46 residues (also called the KEKE motif) ( xref )."

No evidence text available

sparser
"The complexes varied from very stable machines to relatively transient interactions, such as the binding of UCHL5 and ADRM1 to the proteasome xref ."

reach
"Proteasome-ubiquitin receptor hRpn13 and Adrm1 binds and activates deubiquitinating enzyme Uch37 and UCHL5 and is targeted by bis-benzylidine piperidone RA190, which restricts cancer growth in mice xenografts."

sparser
"The C-terminal domain of UCH37 associates with C-terminus of the lid subunit Adrm1 ( xref , xref , xref )."

sparser
"NF-κB activity is dependent on the RPN13-UCH37 axis in the proteasome because it contributes to the recognition of polyUb-tagged IκBα as a substrate for the proteasome."

sparser
"Similarly, the peripherally associated proteasome DUBs Ubp6 and Uch37 are located adjacent to different ubiquitin receptors: Uch37 binds the proteasome through Rpn13, whereas the UBL of Ubp6 is tethered to Rpn1 at the T2 site that is distinct from the T1 ubiquitin binding site ( xref , xref , xref , xref )."

sparser
"Ubiquitin receptors play an integral role in substrate capture and apparently contribute to ubiquitin chain deconjugation, as Rpn13 binds and activates deubiquitinating enzyme Uch37 ( xref ; xref ; xref )."

reach
"There is an interaction between Uch2/Uch37 and the proteasomal Ub receptor Rpn13."

sparser
"Association of UCH37 with Adrm1 increases the efficiency of hydrolysis of an artificial substrate, Ub-AMC, by decreasing the K M for the substrate without modifying the V max ( xref )."

sparser
"Interaction of Adrm1 with Uch37 increased the production of triubiquitin (Ub3), diubiquitin (Ub2), and monoubiquitin (Ub1) ( xref )."

sparser
"Higher eukaryotes express an additional DUB, UCH37, which binds to a domain of Rpn13 that is only found in organisms with an UCH37 gene [ xref , xref , xref , xref , xref , xref ]."

sparser
"Uch37 was activated by Adrm1 to form Uch37Adrm1 complex, exhibiting 12-fold higher activity than Uch37 alone ( xref )."

sparser
"The structure of Calypso–ASX is reminiscent of the activated deubiquitinase complex observed for UCH-L5 bound to the Deubad domain of Rpn13 (Supplementary Fig.  xref , left panel) (PDB codes: 4UEM and 4WLQ), rather than the inhibitory Deubad INO80G bound to the same UCH DUB (Supplementary Fig.  xref , right panel) (PDB codes: 4UF5 and 4WLP) xref , xref ."

sparser
"The interaction between RPN13 and UCH37 is mediated by the C-terminal DEUBAD domain of RPN13 and the C-terminal UCH37-like domain (ULD) of UCH37 [ xref ]."

sparser
"To evaluate TA derivatives with a complex of UCHL5 and Rpn13, UCHL5 (0.464 nM) and RPN13 (915 nM) were used in the presence of individual TA derivative (100 μM)."

reach
"This is similar to what was previously observed for the interaction between Uch37 and hRpn13, the proteasome subunit that binds Uch37 via the C-terminal tail to recruit it to the 19S RP."

reach
"This interaction does not affect the interaction between UCH37 and ADRM1 (Figure 3E)."

reach
"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."

reach
"Consistent with our previous report that hRpn13 activates Uch37, the Uch37 and hRpn13 complex reacts with UbVS more rapidly than Uch37 alone (XREF_FIG)."

sparser
"Usp14 (yeast UBP6) is associated with Rpn1 xref and Uch37 binds to the C-terminal domain of Rpn2-bound Rpn13; i.e., Uch37 associates with the base via Rpn13. xref , xref Intriguingly, deubiquitylation by Uch37 is activated by proteasome binding, which is also involved in the editing of polyubiquitin chains."

reach
"Thus, hRpn13 activates hINO80 associated Uch37 without displacing it from the hINO80 complex, and activation is a consequence of transient interactions between Uch37 and hRpn13."

sparser
"Based on these results, we hypothesized that binding of pro-SFTPB to ADRM1 suppresses hRpn2 binding to ADRM1 and thereby inhibits ADRM1 activation and the interaction between ADRM1 and UCH37."

sparser
"As expected, unlike overexpression of wild-type pro-SFTPB, overexpression of pro-SFTPB mutated at the ADRM1 binding site did not affect the interaction of ADRM1 with hRpn2 or the interaction of ADRM1 with UCH37 (Fig.  xref d)."

sparser
"Taken together, these findings suggest that pro-SFTPB inactivates ADRM1 by blocking the binding of hRpn2 and UCH37 to ADRM1, thereby inhibiting the deubiquitination of PGK1 by ADRM1 and ultimately leading to ubiquitination and degradation of PGK1."

sparser
"We also demonstrate that pro-SFTPB inhibits the interaction of ADRM1 with hRpn2 by binding directly to ADRM1 and that the interaction between pro-SFTPB and ADRM1 also inhibits the interaction between ADRM1 and UCH37."

sparser
"This result is in agreement with the report of xref who also found that RA190 had no effect on Uch37-Rpn13 interactions using a different assay."

sparser
"Our strategies for targets 98 and 99, RPN13-UCH-L5 binding, were based on the observation that RPN13 bound to the KEKE motif at the C-terminal end of UCH-L5. xref Through ZDOCK’s blocking feature we restricted binding to the C-terminus, and the bound structures showed that this assumption was correct."

reach
"25 showed that Adrm1 binds two proteasome subunits, S1/Rpn2 and the deubiquitinylating enzyme Uch37."

reach
"The full-length UCH37 shows a low isopeptidase activity, however, the activities of the UCH-domain only or of the UCH37 and Adrm1 complex are two orders of magnitude higher than that of the full-lengt[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Rather, their positions were inferred through their interactions: Usp14/Ubp6 was found to bind Rpn1 [ xref ], and Uch37 could bind both Adrm1 and S5a/Rpn10 [ xref , xref , xref , xref ]."

reach
"Interestingly, USP14 and UCH37 bind to RPN1 and to RPN13, respectively, which are, in addition to the RPN10, substrate receptors of the 19S regulatory particle [67], which provide a versatile binding platform for various ubiquitin chains [68]."

sparser
"Adrm1 interacts with the C-terminus of UCH37 via a C-terminal domain, which is absent in S. cerevisiae Rpn13."

No evidence text available

No evidence text available

sparser
"It has been reported that ADRM1 (human Rpn13 [hRPN13]) binds this region of UCHL5 and relieves its deubiquitinase activity, accelerating the hydrolysis of ubiquitin-7-amido-4-methylcoumarin (Ub-AMC)."

No evidence text available

reach
"The result indicated that hRpn13 interacted with Uch37 equivalently when RA190 was present (XREF_FIG, lane 3 versus 2)."

reach
"The complete C-terminal portion of Adrm1 binds the unique C-terminal tail of UCH37 which inhibits its catalytic activity."

reach
"Since Uch37 interaction with hRpn13 appeared to be unaffected by RA190, we hypothesized that the presence of Uch37 at the proteasome would similarly be unperturbed by RA190."

sparser
"In vitro binding of Uch37 with Rpn13 was shown to promote the hydrolysis of ubiquitin-7-amido-4-methylcoumarin (Ub-AMC) and Uch37's reactivity with suicide inhibitors such as ubiquitin vinylsulfone (UbVS) and ubiquitin aldehyde (Ubal). xref Activation appeared to be regulated in part by the C-terminal domain of Uch37, xref as removal of the residues 238-329 provided enhanced hydrolase activity."

reach
"This suggests that a specific interaction between UCH37 and ADRM1 occurs and we can hypothesise that this role of TsUCH37, releasing Ub from proteins targeted for degradation, has been conserved throughout evolution."

reach
"We report that RA190 reacts with hRpn13 DEUBAD domain C357 (XREF_FIG, XREF_TABLE and XREF_SUPPLEMENTARY); however, this cysteine is directed away from the Uch37 binding surface and does not appear to effect Uch37 interaction with hRpn13 (XREF_FIG) or the proteasome (XREF_FIG)."

sparser
"Since UCHL5 binds to hRpn13 DEUBAD, and MGMT responded similarly to UCHL5 following hRpn13-editing, we tested whether MGMT and hRpn13 interact in cells."

sparser
"UCH37 bind tightly to the 26S proteasome through Rpn13."

sparser
"Binding of Rpn13 to Uch37 increases the isopeptidase activity of Uch37; therefore it may facilitate the rescue of ubiquitinated substrates from proteolysis xref , xref , xref ."

No evidence text available

No evidence text available

No evidence text available

No evidence text available

sparser
"When UCH37 is bound to RPN13 alone or in the context of the proteasome, the rate of debranching is dramatically enhanced."

sparser
"RA190 does not affect hRpn13 interaction with Uch37, but rather directly binds and inactivates Uch37."

sparser
"Therefore, the external stimuli of exogenous rHcADRM1 may hamper the ADRM1-Uch37 interaction in host T cells, disrupt the balance of cell cycle protein degradation and interfere with ADRM1 substrate IκBα signaling along with its downstream effectors [ xref , xref ]."
| PMC

reach
"Alanine substitutions of Val286, Asp287, Glu295, and Ile296 or of Lys371, Asp373, Glu375, and Lys379 reduces (XREF_FIG, Lane 2) or abrogates (XREF_FIG, lane 4) hRpn13 binding to Uch37."

reach
"Yeast and human Uch37 bind the noncatalytic protein Adrm1 and thereby become more active ( Qiu et al., 2006; Yao et al., 2006 )."

reach
"The two domains may become constrained by the simultaneous binding of Uch37 and hRpn13 's Pru domain to different ubiquitin moieties within a chain."

reach
"However, the binding of Adrm1 to Uch37 did not increase the k cat value, but rather led to 6-fold decrease in K M , seemingly promoting recruitment of the enzyme to the substrate ( Qiu et al., 2006; Y[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Notably, similar to the RPN13-UCHL5 interaction, these factors also use their DEUBAD to interact with the CTD of BAP1 (see above)."

No evidence text available

No evidence text available

No evidence text available

No evidence text available

No evidence text available

sparser
"In mammalian cells, association of UCHL5 with RPN13 has been reported to activate UCHL5 ( Yao et al., 2006 )."

sparser
"For example, it was demonstrated that the RPN13-UCHL5 complex promotes degradation of inducible nitric oxide synthase (iNOS), while stabilizing NFκB suppressor IκBα ( xref )."

No evidence text available

No evidence text available

No evidence text available

reach
"Since UCHL5 binds to hRpn13 DEUBAD, and MGMT responded similarly to UCHL5 following hRpn13-editing, we tested whether MGMT and hRpn13 interact in cells."

No evidence text available

No evidence text available

reach
"According to literature [ 14 , 15 ], ADRM1 could bind to UCH37 and activate the deubiquitination activity of UCH37 through tool cells."

reach
"By co-immunoprecipitation with ADRM1 or UCH37, we further confirmed that ADRM1 could bind to UCH37 in ATDC5 cells ( Fig. 7 A and B ), and ADRM1 overexpression significantly enhanced the interaction of[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"A similar mechanism of action, involving Rpn13, has been suggested for EF24. xref Rpn13 is known to bind and to activate the DUB UCHL5, and it was subsequently shown that RA-190 does not affect the interaction of Rpn13 with UCHL5 but directly inactivates UCHL5. xref "

reach
"ADRM1UCH37 interaction not only activated UCH37 activity but was also important for UCH37 stability.Previous literature has reported that ADRM1 could bind to UCH37 and activate its deubiquitination a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"Next, in 2006, three independent groups confirmed that ADRM1 is a novel 19S proteasome cap-related protein, and they further found ADRM1 interacts with UCH37 and recruits it to the proteasome, thereby[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"According to previous literature, it has been established that ADRM1 bind to UCH37 to activate its deubiquitination activity in HEK293 cell [ 26 , 28 ]."

sparser
"To test the impact of RA190 on hRpn13 interaction with Uch37, we evaluated whether Uch37 is crosslinked to hRpn13 in RA190-treated cells, by using a denaturing immunoprecipitation experiment."

sparser
"However, we showed that ADRM1UCH37 interaction was important for UCH37 stability."

sparser
"To test further whether RA190 disrupts hRpn13 interaction with Uch37, we used an in vitro pulldown experiment."

sparser
"Rpn13 can interact with Uch37 and recruit it to the proteasome via its C-terminal 46 residues (also called the KEKE motif) and activates Uch37."

sparser
"Second, RPN13 binds to UCH37 on a surface that includes the active-site crossover loop ( xref ; xref ), a feature of all UCH DUBs that plays a crucial role in regulating access to the canonical active site of the enzyme."

No evidence text available

No evidence text available

sparser
"Furthermore, it is known that the Rpn13 C-terminal domain can interact with Uch37 via its KEKE motif and activate Uch37 in a manner similar to that of the full-length Rpn13."

sparser
"Taken together, the SEC, AUC, and SAXS analyses of different concentrations of Uch37 suggested that Uch37 could exist as a mixture of different oligomeric states in solution and Uch37 was de-oligomerized in the presence of Rpn13, forming a stable heterodimer of Rpn13 and Uch37."

No evidence text available

sparser
"The binding of Rpn13 to the KEKE motif of Uch37 likely perturbs the hydrophobic interactions of tetrameric Hc, resulting in disassembly of the oligomer into a monomer via the formation of a stable Rpn13-Uch37 complex that provides a means to keep Uch37 in the monomeric state."

reach
"Uch37 was activated by Adrm1 to form Uch37 and Adrm1 complex, exhibiting 12-fold higher activity than Uch37 alone."

sparser
"Because of their shared domain architecture, our current understanding of PR-DUB catalytic activity is built upon both recent crystal structures of the Drosophila PR-DUB complex and prior structures of the UCHL5Rpn13 complex."

sparser
"Structures of UCH-L5-Rpn13 bound to ubiquitin are available."

sparser
"The region in Uch37 that interacts with hRpn13 is aggregation prone xref xref xref and it is possible that the small reduction of Uch37 immunoprecipitated with hRpn13 in RA190-treated cells is caused by nonspecific interactions with this region when RA190 is adducted to the Uch37 catalytic domain."

sparser
"Uch37 binds proteasomes through its C-terminal Uch37-like domain (ULD), which is recognized by proteasome subunit Rpn13 ( xref )."

sparser
"The result indicated that hRpn13 interacted with Uch37 equivalently when RA190 was present ( xref , lane 3 versus 2)."

sparser
"Since Uch37 interaction with hRpn13 appeared to be unaffected by RA190, we hypothesized that the presence of Uch37 at the proteasome would similarly be unperturbed by RA190."

sparser
"We also demonstrated that Rpn13C (Rpn13 residues 270–407) could disrupt the oligomerization of Uch37 by sequestering Uch37 and forming a Uch37-Rpn13 complex."

No evidence text available

sparser
"According to literature [ 14 , 15 ], ADRM1 could bind to UCH37 and activate the deubiquitination activity of UCH37 through tool cells."

sparser
"By co-immunoprecipitation with ADRM1 or UCH37, we further confirmed that ADRM1 could bind to UCH37 in ATDC5 cells ( Fig. 7 A and B ), and ADRM1 overexpression significantly enhanced the interaction of[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"ADRM1UCH37 interaction not only activated UCH37 activity but was also important for UCH37 stability."

sparser
"Previous literature has reported that ADRM1 could bind to UCH37 and activate its deubiquitination activity, and UCH37 could deubiquitinate and stabilize ALK5 [ 14 , 15 , 22 , 23 ]."

reach
"UPS14 interacts with RPN1, while UCH37 binds to ADRM1 and RPN13 XREF_BIBR XREF_BIBR."

sparser
"Next, in 2006, three independent groups confirmed that ADRM1 is a novel 19S proteasome cap-related protein, and they further found ADRM1 interacts with UCH37 and recruits it to the proteasome, thereby[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"According to previous literature, it has been established that ADRM1 bind to UCH37 to activate its deubiquitination activity in HEK293 cell [ 26 , 28 ]."

reach
"The complexes varied from very stable machines to relatively transient interactions, such as the binding of UCHL5 and ADRM1 to the proteasome 8."

sparser
"We provided several aspects of evidence for ADRM1 in the regulation of UCH37 expression and ADRM1 interaction with UCH37, leading to activate its deubiquitination activity while increased and activate[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"When the proteasome subunit RPN13, which has a deubiquitylase adaptor domain (DEUBAD), binds UCHL5, it stabilizes the flexible active site crossover loop in a catalytically productive conformation to [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"RPN2 interacts with RPN13, a protein that binds the Ub-dependent hydrolase UCH37 and is incorporated in some but not all proteasome particles [16] ."

reach
"When the proteasome subunit RPN13, which has a deubiquitylase adaptor domain (DEUBAD), binds UCHL5, it stabilizes the flexible active site crossover loop in a catalytically productive conformation to [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

No evidence text available

sparser
"The deubiquitinase UCH37 binds to ADRM1 through its DEUBAD domain at the proteasome."

No evidence text available

sparser
"Furthermore, Rpn13 did not stably bind Uch37 when Uch37 was complexed with INO80."

No evidence text available

No evidence text available

reach
"The proteasome has two additional DUBs, Ubp6/USP14 and UCHL5/Uch37, which bind to Rpn1 and Rpn13, respectively."

No evidence text available

reach
"First, the UCH37/RPN13 complex binds to both distal ubiquitin subunits that emanate from the branch point of a K6/K48 chain to increase the affinity of the enzyme for the branch point (Song et al., 2021) (Figure 1D)."

reach
"Second, RPN13 binds to UCH37 on a surface that includes the active-site crossover loop (Sahtoe et al., 2015; VanderLinden et al., 2015), a feature of all UCH DUBs that plays a crucial role in regulating access to the canonical active site of the enzyme."

sparser
"This interaction does not affect the interaction between UCH37 and ADRM1 (Figure xref )."

No evidence text available

No evidence text available

No evidence text available

No evidence text available

sparser
"Activation most likely is achieved by facilitating substrate access, as we showed that association of Uch37 with hRpn13 lowers the K m for UbAMC without affecting k cat ."

sparser
"In contrast to a previous report, we find that RPN13 binds ubiquitin with an affinity similar to that of other proteasome-associated ubiquitin receptors and that RPN2, ubiquitin, and the deubiquitylase UCH37 bind to RPN13 with independent energetics."

No evidence text available

reach
"The hRpn13 and UCH37 complex hydrolyzes large Ub conjugates with incorporation into the 19S complex."

reach
"Pro-SFTPB inhibits ADRM1/UCH37 complex formation by inhibiting hRpn2 binding to ADRM1."

sparser
"As with the case of Uch37 binding to Rpn13, Ubp6 is activated by association with Rpn1 ( xref ), and Ubp6 also seems to modify 19S RP structure because its binding delays proteolysis by a mechanism that is independent of its catalytic activity ( xref )."

sparser
"With the exception of the shorter Rpn13 protein from S. cerevisiae , Rpn13 binds the DUB Uch37 and thereby recruits it to the proteasome's RP xref - xref ."

sparser
"These properties explain HR23a's ability to inhibit substrate deubiquitylation and are markedly different from Rpn13's binding to and activation of the proteasomal DUB Uch37."

No evidence text available

sparser
"The synthesis for FRF hairpin structure of NFRKB may competitively bind UCHL5 with RPN13, inhibit the deubiquitase activity of UCHL5."

sparser
"Yeast and human Uch37 bind the noncatalytic protein Adrm1 and thereby become more active ( Qiu et al., 2006; Yao et al., 2006 )."

sparser
"Uch37 (also known as UCHL5) binds to the C-terminal domain of Rpn13, which activates it and brings it in proximity to RP-bound substrates xref , xref , xref ."

sparser
"The Adrm1-UCH37 interaction recruits UCH37 to the proteasome and activates its deubiquitination activity."

sparser
"However, the binding of Adrm1 to Uch37 did not increase the k cat value, but rather led to 6-fold decrease in K M , seemingly promoting recruitment of the enzyme to the substrate ( Qiu et al., 2006; Y[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"ADRM1 binds the C-terminal tail of UCHL5 resulting in a conformational change that relieves auto-inhibition of the catalytic active site (Yao et al., 2008; Qiu et al., 2006)."

reach
"The deubiquitinating enzyme complex ADRM1-UCHL5 promotes filopodia formation in liver cancer cells by stabilizing FASN."

sparser
"Ubiquitin is spacially accommodated by partial melting of a UCH domain helix and xref and xref find that this state is also adopted when UCH37 is bound to RPN13."

reach
"Based on these results, we hypothesized that binding of pro-SFTPB to ADRM1 suppresses hRpn2 binding to ADRM1 and thereby inhibits ADRM1 activation and the interaction between ADRM1 and UCH37."

reach
"On the one hand, low expression of SIAH1 can trigger FASN to undergo deubiquitination and escape from proteasomal degradation through ADRM1-UCHL5 complex."

sparser
"And both the protein levels of ADRM1-UCHL5 and ADRM1-FASN presented a direct correlation in normal and liver cancer specimens (Fig. xref )."

sparser
"These results suggest that ADRM1-UCHL5 could promote the deubiquitination of FASN and there is a direct correlation between them in clinical expression."

reach
"We also demonstrate that pro-SFTPB inhibits the interaction of ADRM1 with hRpn2 by binding directly to ADRM1 and that the interaction between pro-SFTPB and ADRM1 also inhibits the interaction between ADRM1 and UCH37."

No evidence text available

sparser
"The deubiquitinating enzyme complex ADRM1-UCHL5 promotes filopodia formation in liver cancer cells by stabilizing FASN."

sparser
"Interestingly, the formation of isolated Uch37Adrm1 complexes does not lead to activation hinting at a more complex mechanism."

sparser
"HDAC8 interaction does not affect the UCH37-ADRM1 interaction."

No evidence text available

sparser
"On the one hand, low expression of SIAH1 can trigger FASN to undergo deubiquitination and escape from proteasomal degradation through ADRM1-UCHL5 complex."

No evidence text available

reach
"The interaction of human UCH37 and ADRM1 was used as a reference for the accuracy of the prediction ,yielding a pTM score of 0.79 and ipTM of 0.83."

reach
"It has been reported that ADRM1 (human Rpn13 [hRPN13]) binds this region of UCHL5 and relieves its deubiquitinase activity, accelerating the hydrolysis of ubiquitin-7-amido-4-methylcoumarin (Ub-AMC)."

No evidence text available

No evidence text available

No evidence text available

No evidence text available

sparser
"Rpn13 binds with high-affinity ubiquitin carboxyl-terminal hydrolase L5 (UCHL37), the deubiquitinating enzyme that helps with ubiquitin (Ub) hydrolysis[ xref ]."

sparser
"Single channel current measurements of MspA were separately performed in the presence of Ub, ubiquitin dimer (di-Ub), ubiquitin trimer (tri-Ub), and UCH37 bound to its partner protein RPN13 ( xref – xref )."

No evidence text available

sparser
"We then demonstrated that pro-SFTPB suppresses the formation of the ADRM1/hRpn2/UCH37 complex by binding to ADRM1, which inhibits PGK1 deubiquitination, thus accelerating ubiquitin-mediated PGK1 degradation."

sparser
"As PSMD1 (scRpn2) encodes for the largest non-ATPase subunit of the 19S regulator lid of the 26S proteasome and this is involved in binding to the deubiquitinase UCH37 (scUCHL5) via the adapter protein ADRM1 (scRpn13), we hypothesized that knockout of PSMD1 may be disrupting the binding of UCH37 to the 26S proteasome, thereby inhibiting its deubiquitinase activity and leading to HIV-1 reactivation xref (Fig.  xref )."