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UCHL5 binds Proteasome. 36 / 41
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"Considering that UCH-L5 is associated with the proteasome, where the local concentration of ubiquitin is much higher than the average cellular concentration, UCH-L5 might effectively deubiquitinate its substrates for editing purposes before the substrates are degraded by the proteasome."
28338014
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"UCHL5 forms a reversible association with the proteasome by binding to the 26S proteasome via the Admr1 receptor in the 19S RP base complex; this enhances the isopeptidase activity of the enzyme [79] [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
29864528
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"It was initially believed that the presence of DUBs at the proteasome (such as Uch37/UchL5 and Usp14) would promote the degradation of proteins through facilitating substrate processing (see also the next section)"
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"Potential homologues of Rad23 (encoded by At1g16190, At1g79650, At3g02540 and At5g38470) and UCH37 [15] are encoded by the Arabidopsis genome, however, no RPN13-like plant proteins could be found, sug[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
17825468
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"The association of UCH-L5 with the 26S proteasome makes it an interesting target for high throughput screening assays."
35720124
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"UCHL5 is associated with the 26S proteasome, where it serves to remove distal ubiquitin moieties from polyubiquitylated proteins."
33097533
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"The deubiquitinating enzyme UCH-L5 is associated with 26S proteasome, where it removes distal Ub moieties from polyubiquitinated proteins ( xref ), and it is specific to K48-linked polyUb chains ( xref )."
37841261
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"Proteasome-Bound UCH37 Debranches Chains."
33156996
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"In direct contrast to the proteasome-bound UCH37 enzyme, isopeptidase T disassembles ubiquitin oligomers from the free “proximal” end, i.e., the end with an unattached Gly76 carboxyl group."
15571815
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"Kinetics of Proteasome-Bound UCH37 Resemble the UCH37•RPN13 Complex."
33156996
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"The recruitment of UCH37 to the proteasome is mediated by the C-terminal region of Rpn13, indicating that substrate recognition and ubiquitin-chain processing might be coupled."
26169395
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"Functionally, UCHL5 recruitment to the proteasome ensures poly-Ub chain debranching, enhancing proteasomal degradation, and promoting proper cell cycle progression (112, 113)."
35764170
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"UCH37 associates with the proteasome through Rpn13 and promotes efficient degradation of substrates ( xref ; xref ; xref )."
38517379
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"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)."
28598414
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"In direct contrast to the proteasome-bound UCH37 enzyme, isopeptidase T disassembles ubiquitin oligomers from the free “proximal” end, i.e., the end with an unattached Gly76 carboxyl group."
15571815
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"Binding of UCHL5 to the proteasome repositions a crossover loop, thereby relieving an auto-inhibitory effect and allowing substrate access to the active site 48."
26918171
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"Deubiquitinating enzyme UCHL5 associates with proteasome in processing polyubiquitinated protein substrates and has been shown to elevate in muscle atrophy induced by diabetes [46 , 47] and denervatio[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
36681307
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"Proteasome bound UCH37 is thought to behave as an " editor ", relieving poorly ubiquitinated substrates from degradation by sequentially dismantling their K48 linked polyubiquitin chains from the very distal end, removing one ubiquitin at a time."
23617878
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"A recent study proposed that proteasome associated UCH37 can debranch ubiquitin chains to promote substrate degradation [XREF_BIBR]."
32726943
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"Uch37 and Usp14 associate reversibly with the proteasome, whereas Rpn11 is a stoichiometric subunit XREF_BIBR."
20829789
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"Deubiquitinating enzyme UCHL5 associates with proteasome in processing polyubiquitinated protein substrates and has been shown to elevate in muscle atrophy induced by diabetes [46 , 47] and denervatio[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
36681307
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"In the most well-known example, the three DUBs, RPN11, USP14, and UCHL5, bind to the proteasome to deubiquitinate proteins substrates destined to degradation, thus recycling the ubiquitin molecules (99)."
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"Of these proteasome-associated DUBs, Rpn-11 is a subunit of the proteasome, whereas Uchl5 and Usp14 bind to the proteasome (reviewed in Collins and Goldberg, 2017; Finley, 2009; and Kocaturk and Gozuacik, 2018)."
39912491
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"UCHL5/Uch37 binds to the proteasome through hRpn13, with its ULD domain enveloped by a C-terminal deubiquitinase adaptor (DEUBAD) domain in Rpn13 [60,61] (Figure 3C)."
35817651
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"Human UCH37 interacts with both the proteasome, via Rpn13, and the INO80 complex in the nucleus via NFRKB."
39604441
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"Notably, Rpn11 is an integral subunit of the 19S regulatory particle whereas Uch37 and USP14 associate reversibly with the proteasome (Hung et al., 2022; Zhang et al., 2022)."
38455765
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"The DUBs Ubiquitin-Specific Protease 14 (USP14) and Ubiquitin Carboxyl-terminal Hydrolase L5 (UCHL5/UCH37) associate with the proteasome to deubiquitinate incoming substrates to limit their degradation [ xref ]."
33414510
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"We also highlight new findings concerning the formation of branched chains in response to small molecules that induce the degradation of otherwise stable proteins and examine the selective debranching of heterotypic chains by the proteasome-bound deubiquitylase UCH37."
37325469
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"The p97 proteome also contained many proteasome subunits, but not the proteasome‐associated DUBs Rpn11/PSMD14, Ubp6/USP14 or UCH37/UCHL5 (Collins & Goldberg, 2017)."
31613024
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"We used NAC, a thiol containing compound, to block the active site of auranofin and found NAC recovers most auranofin mediated DUB inhibition to purified 26S proteasome, which confirms the computational model results that auranofin targets proteasome associated UCHL5 and USP14."
26097878
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"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 )."
32210344
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"UCHL5 reversibly associates with the 26S proteasome and prevents target proteins degradation by hydrolyzing ubiquitin chains ( xref )."
32596150
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"UCH37 (also known as UCH-L5), the third member of the UCH gene family, contains a short C-terminal extension and associates with the proteasome and the INO80 chromatin remodeling complex [XREF_BIBR - XREF_BIBR]."
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"17 Of the three, USP14 and UCHL5 reversibly associate with the proteasome, whereas the third, RPN11 and POH1, is an intrinsic component of the lid subcomplex of the 19S cap."
27813535
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"Proteasome-bound UCH37 is known to exhibit poor DUB activity for isopeptide-linked ubiquitin–protein conjugates, despite showing predominant activity over USP14 against ubiquitin adducts with small leaving groups, such as ubiquitin amidomethylcoumarin (UbAMC) [ xref , xref ]."
32726943
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"Proteasome bound UCH37 is known to exhibit poor DUB activity for isopeptide linked ubiquitin protein conjugates, despite showing predominant activity over USP14 against ubiquitin adducts with small leaving groups, such as ubiquitin amidomethylcoumarin (UbAMC) [XREF_BIBR, XREF_BIBR]."
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