Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26S Proteasome

By R. Verma, L. Aravind, Robert S. Oania, W. McDonald, John R. Yates III, Eugene V. Koonin, R. Deshaies. Science, 2002

1,087 citations recorded by the source corpus.

Subfields: Epidemiology, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/cd471f6893929d67794312ed1c8e1533e6202782

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Citations in the corpus

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).”
p62 links the autophagy pathway and the ubiqutin–proteasome system upon ubiquitinated protein degradation (2016, neutral): “substrate recognition, deubiquitination, unfolding and further translation into 20S for degradation [7, 8].”
Regulation and Cellular Roles of Ubiquitin-specific Deubiquitinating Enzymes (2009, background): “A third DUB, Rpn11 in yeast and POH1 in humans, is an integral part of the 19S regulatory particle (87, 142).”
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 .”
A genomic and functional inventory of deubiquitinating enzymes. (2005, neutral): “Furthermore, although some circumstantial evidence indicates that CSN5 may contain Ub protease activity, its main proteolytic target is thought to be the Ubl NEDD8 (Groisman et al., 2003; Verma et al., 2002; Yao and Cohen, 2002).”
The Logic of the 26S Proteasome. (2017, positive): “Inmost eukaryotes, there are three major DUBs associated with the proteasome: the metalloprotease Rpn11 (Verma et al., 2002; Yao and Cohen, 2002) and the cysteine proteases, Usp14 (Ubp6 in S.”
The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. (2003, positive): “…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).”
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.”