Role of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of Nedd8 from Cul1

By G. Cope, Greg S. B. Suh, L. Aravind, Sylvia E. Schwarz, S. Zipursky, Eugene V. Koonin, R. Deshaies. Science, 2002

732 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/56b88e419f32424ab4eb08639479f2caddaa5179

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In Cell Biology

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Citations in the corpus

Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome (2009, background): “Subunit Csn5, a paralog of Rpn11, carries the metalloprotease active site (90).”
Regulation and Cellular Roles of Ubiquitin-specific Deubiquitinating Enzymes (2009, background): “F or p er so na l u se o nl y. ANRV378-BI78-14 ARI 29 April 2009 13:16 ubiquitinated substrates (87–90), and one acts on proteins modified with the ubiquitin-like modification Nedd8 (86).”
A genomic and functional inventory of deubiquitinating enzymes. (2005, unknown): “Indeed, it was recently described that a previously unnoticed Ub-interacting Zinc finger domain in USP15 is needed for disassem- Cell 123, December 2, 2005 ©2005 Elsevier Inc. 779 Figure 4.”
Human and mouse proteases: a comparative genomic approach (2003, background): “There are recent examples of experimental work that has led to the unmasking of some of these 'hidden proteases', including: JAMM proteins, which are a new family of deubiquitylating metalloprotease”
CSN controls NF‐κB by deubiquitinylation of IκBα (2007, background): “Most importantly, knockdown of CSN5 resulted in a reduced reaccumulation of IkBa after its TNFa-induced degradation.”
Deubiquitination and Stabilization of PD-L1 by CSN5 (2016, background): “JAMM plays a critical role in CSN complex-mediated deneddylation and further regulates the activity of the Skp, Cullin, F box-containing complex (Cope et al., 2002).”
The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. (2003, background): “Cul4A is a member of the cullin family of the His-X-HIS-X10-Asp metalloprotease motif that functions as a catalytic site for the NEDD8 isopeptidaseubiquitin ligase subunits (also known as E3s) that promote ubiquitin transfer to the substrates, the last step activity (Cope et al., 2002).”