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Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4
Author(s) -
Jäger Sibylle,
Strayle Jochen,
Heinemeyer Wolfgang,
Wolf Dieter H.
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.16.4423
Subject(s) - stuttgart , library science , art history , humanities , art , computer science
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.

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