1932

Abstract

Protein degradation is deployed to modulate the steady-state abundance of proteins and to switch cellular regulatory circuits from one state to another by abrupt elimination of control proteins. In eukaryotes, the bulk of the protein degradation that occurs in the cytoplasm and nucleus is carried out by the 26S proteasome. In turn, most proteins are thought to be targeted to the 26S proteasome by covalent attachment of a multiubiquitin chain. Ubiquitination of proteins requires a multienzyme system. A key component of ubiquitination pathways, the ubiquitin ligase, controls both the specificity and timing of substrate ubiquitination. This review is focused on a conserved ubiquitin ligase complex known as SCF that plays a key role in marking a variety of regulatory proteins for destruction by the 26S proteasome.

Keyword(s): Cdc34F boxSkp1ubiquitinubiquitination
Loading

Article metrics loading...

/content/journals/10.1146/annurev.cellbio.15.1.435
1999-11-01
2024-12-04
Loading full text...

Full text loading...

/content/journals/10.1146/annurev.cellbio.15.1.435
Loading
/content/journals/10.1146/annurev.cellbio.15.1.435
Loading

Data & Media loading...

  • Article Type: Review Article
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error