| Literature DB >> 11500370 |
S Jäger1, J Strayle, W Heinemeyer, D H Wolf.
Abstract
In eukaryotes, the ubiquitin-proteasome system plays a major role in selective protein breakdown for cellular regulation. Here we report the discovery of a new essential component of this degradation machinery. We found the Saccharomyces cerevisiae protein Cic1 attached to 26S proteasomes playing a crucial role in substrate specificity for proteasomal destruction. Whereas degradation of short-lived test proteins is not affected, cic1 mutants stabilize the F-box proteins Cdc4 and Grr1, substrate recognition subunits of the SCF complex. Cic1 interacts in vitro and in vivo with Cdc4, suggesting a function as a new kind of substrate recruiting factor or adaptor associated with the proteasome.Entities:
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Year: 2001 PMID: 11500370 PMCID: PMC125261 DOI: 10.1093/emboj/20.16.4423
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598