ArticleProtein & cell2014
Mechanism of the Rpn13-induced activation of Uch37.
Article in Protein & cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Interactions Between E3 Ubiquitin Ligases and Deubiquitinases in AKT Regulation: Implications in Skeletal Muscle Homeostasis.Cell biochemistry and function · 2026Review
- Bromodomain proteins IBD1 and IBD2 link histone acetylation to SWR1- and INO80-mediated H2A.Z regulation in Tetrahymena.Epigenetics & chromatin · 2025Article
- UCHL3: a crucial deubiquitinase in DNA damage repair and tumor progression.Cancer cell international · 2025Review
- Prediction of Disordered Linkers Using APOD.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Proteasome associated function of UCH37 is evolutionarily conserved in Plasmodium parasites.Scientific reports · 2024Article
- Downregulation of pro-surfactant protein B contributes to the recurrence of early-stage non-small cell lung cancer by activating PGK1-mediated Akt signaling.Experimental hematology & oncology · 2023Article
- Development and anticancer properties of Up284, a spirocyclic candidate ADRM1/RPN13 inhibitor.PloS one · 2023Article
- Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies.The FEBS journal · 2021Review
- DUBs Activating the Hedgehog Signaling Pathway: A Promising Therapeutic Target in Cancer.Cancers · 2020Review
- Structure-function analyses of candidate small molecule RPN13 inhibitors with antitumor properties.PloS one · 2020Article
- Ubiquitin C-Terminal Hydrolase L5 (UCHL5) Accelerates the Growth of Endometrial Cancer via Activating the Wnt/β-Catenin Signaling Pathway.Frontiers in oncology · 2020Article
- The multiple roles of deubiquitinases in liver cancer.American journal of cancer research · 2020Review
- Monoubiquitination of ASXLs controls the deubiquitinase activity of the tumor suppressor BAP1.Nature communications · 2018Article
- A fluorescence polarization-based competition assay for measuring interactions between unlabeled ubiquitin chains and UCH37•RPN13.Analytical biochemistry · 2018Article
- Quantitative Proteomic Analysis Reveals That Arctigenin Alleviates Concanavalin A-Induced Hepatitis Through Suppressing Immune System and Regulating Autophagy.Frontiers in immunology · 2018Article
- Meddling with Fate: The Proteasomal Deubiquitinating Enzymes.Journal of molecular biology · 2017Review
- Protein Degradation Systems as Antimalarial Therapeutic Targets.Trends in parasitology · 2017Review
- Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets.Nature communications · 2017Article
- Mechanism of UCH-L5 activation and inhibition by DEUBAD domains in RPN13 and INO80G.Molecular cell · 2015Article
- Structural plasticity allows UCH37 to be primed by RPN13 or locked down by INO80G.Molecular cell · 2015Article
Corrections and comments
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Authors and funding
15 authors at 8 institutions in 3 countries.
Funding
Abstract
Uch37 is a de-ubiquitinating enzyme that is activated by Rpn13 and involved in the proteasomal degradation of proteins. The full-length Uch37 was shown to exhibit low iso-peptidase activity and is thought to be auto-inhibited. Structural comparisons revealed that within a homo-dimer of Uch37, each of the catalytic domains was blocking the other's ubiquitin (Ub)-binding site. This blockage likely prevented Ub from entering the active site of Uch37 and might form the basis of auto-inhibition. To understand the mode of auto-inhibition clearly and shed light on the activation mechanism of Uch37 by Rpn13, we investigated the Uch37-Rpn13 complex using a combination of mutagenesis, biochemical, NMR, and small-angle X-ray scattering (SAXS) techniques. Our results also proved that Uch37 oligomerized in solution and had very low activity against the fluorogenic substrate ubiquitin-7-amino-4-methylcoumarin (Ub-AMC) of de-ubiquitinating enzymes. Uch37Δ(Hb,Hc,KEKE), a truncation removal of the C-terminal extension region (residues 256-329) converted oligomeric Uch37 into a monomeric form that exhibited iso-peptidase activity comparable to that of a truncation-containing the Uch37 catalytic domain only. We also demonstrated that Rpn13C (Rpn13 residues 270-407) could disrupt the oligomerization of Uch37 by sequestering Uch37 and forming a Uch37-Rpn13 complex. Uch37 was activated in such a complex, exhibiting 12-fold-higher activity than Uch37 alone. Time-resolved SAXS (TR-SAXS) and FRET experiments supported the proposed mode of auto-inhibition and the activation mechanism of Uch37 by Rpn13. Rpn13 activated Uch37 by forming a 1:1 stoichiometric complex in which the active site of Uch37 was accessible to Ub.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.