Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4
AUTOR(ES)
Jäger, Sibylle
FONTE
Oxford University Press
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=125261Documentos Relacionados
- RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: A negative feedback circuit
- Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome.
- The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.
- A protein–protein interaction map of the Caenorhabditis elegans 26S proteasome
- Regulation of Repair by the 26S Proteasome