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Review
. 2002 Dec 10;12(23):R815-7.
doi: 10.1016/s0960-9822(02)01317-9.

Ubiquitin system: JAMMing in the name of the lid

Christoph Berndt  1 , Dawadschargal Bech-Otschir, Wolfgang Dubiel, Michael Seeger
Affiliations
Free article
Review

Ubiquitin system: JAMMing in the name of the lid

Christoph Berndt et al. Curr Biol. .
Free article

Abstract

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.

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