In recent years, the ubiquitin/26S proteasome pathway was discovered as a central player for rapid and selective proteolysis in the nucleus and the cytosol. This pathway is not only required for the elimination of misfolded proteins (produced after heat or oxidative stress), but also involved in the degradation of short-lived and key regulatory proteins, which appear to play important roles in a variety of basic cellular processes [Ciechanover et al. (2000) BioEssays 22: 442-451].
Degradation via this pathway is a two-step process (Figure 1): the protein is first tagged by covalent attachment of ubiquitin, and subsequently degraded by a multicatalytic protease complex called the 26S proteasome. Our Network is mainly interested in the functions of two E3 enzymes, the SCF and the APC, which control the cell cycle and different signalling pathways in fungi, plants and animals.