Ubiquitin system: JAMMing in the name of the lid.
The isopeptide bonds formed by ubiquitin or its relatives are cleaved by hydrolases with active site cysteines. Recent studies have revealed that similar metalloprotease motifs--JAMMs--in the Rpn11 subunit of the 26S proteasome lid and in the Csn5 subunit of the COP9 signalosome are involved in deubiquitination and deneddylation, respectively.
Berndt
Christoph
C
Department of Surgery, Division of Molecular Biology, Monbijoustrasse 2, 10117 Berlin, Germany.
Bech-Otschir
Dawadschargal
D
Dubiel
Wolfgang
W
Seeger
Michael
M
D008666:Metalloendopeptidases / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D021122:Protein Subunits; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D015398:Signal Transduction; D025801:Ubiquitin / Q000378:metabolism*
D021122:Protein Subunits; D025801:Ubiquitin; D010447:Peptide Hydrolases; D008666:Metalloendopeptidases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease