A cryptic protease couples deubiquitination and degradation by the proteasome

By T. Yao, R. Cohen. Nature, 2002

776 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/ff43016789f2b0043b9c78c2f6c68b535b3974ad

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Citations in the corpus

The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. (2003, neutral): “…ubiquitin isopeptidease activity, which is re- sponsible for depolymerization of the ubiquitin chainsRNA polymerase IIo has been shown to be very rapidly ubiquitinated after UV irradiation (Bregman et al., 1996; from substrates prior to protein degradation (Verma et al., 2002; Yao and Cohen, 2002).”
Functions and Homeostasis of Zinc, Copper, and Nickel in plants (2005, background): “These activities are required for the biological activities of the respective protein complexes and for the degradation of target proteins (Yao and Cohen 2002).”
Structure and Function of the 26S Proteasome (2018, background): “Rpn11 contains a catalytic zinc ion, coordinated by an EXnHXHX10D metal-binding motif (30, 31), and is absolutely essential for proteasome function and cell viability (152–154).”
Regulation and Cellular Roles of Ubiquitin-specific Deubiquitinating Enzymes (2009, background): “Several groups have reported that mutations affecting the active site of Rpn11/POH1 lead to a loss of viability in Drosophila (143), human cells (59), and yeast (87, 90).”
Breaking the chains: structure and function of the deubiquitinases (2009, background): “Interestingly, JAMM/MPN+ DUBs are commonly found in association with large protein complexes, for example the 26S proteasome -associated PAD1 homologue 1 (also known as POH1 and PSMD14, and homologous to yeast Rpn11”
Systematic exploration of ubiquitin sequence, E1 activation efficiency, and experimental fitness in yeast (2014, background): “Quality filtering of ubiquitin pools by E1 may be particularly important because proteasome-mediated surveillance, an important quality control component for the majority of the proteome 68 , may be unavailable for ubiquitin due to the inherent ubiquitin recycling function of the proteasome 69; 70 .”
Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome (2009, background): “Based on its sequence features, Rpn11 is unlikely to be an ATPase, and this is true as well of the remaining 8 subunits of the Lid.”
Proteasomes and their kin: proteases in the machine age (2004, background): “For example, a folded domain in a model substrate can be denatured in the absence of a polyubiquitin tag — ubiquitin itself was unfolded and degraded following its targeting to proteasomes by fusion to an unfolded polypeptid”
Complete subunit architecture of the proteasome regulatory particle (2012, neutral): “After a substrate binds to an ubiquitin receptor, its poly-ubiquitin chain must be removed by Rpn11 cleavage at the proximal ubiquitin to permit subsequent fast degradation 6,7 .”
A genomic and functional inventory of deubiquitinating enzymes. (2005, neutral): “USP21 and UCH-L3 cleave both Ub and the Ubl molecule NEDD8.”
Mechanism and function of deubiquitinating enzymes. (2004, background): “These residues are essential for the function of the Rpn11 subunit when integrated into the proteasome [23,24,26].”
The Logic of the 26S Proteasome. (2017, neutral): “These structures were solved with and without Usp14, ATPgS, ATP, or ADP-AlFx present or with Rpn11 inactivated to capture a substrate during translocation.”
Deubiquitylating enzymes and drug discovery: emerging opportunities (2017, background): “To facilitate the degradation of proteasome-targeted substrates, these specialized DUBs remove ubiquitin moieties that would otherwise impede entry into the 20S proteasome catalytic core 39 .”