Rising interest in the mechanism and function of the proteasomes and the ubiquitin system
revealed that it is hard to find any aspect of the cellular metabolic network that is not directly …

The elimination of misfolded proteins, known as protein quality control, is an essential
cellular process. Removal of misfolded proteins from the secretory pathway depends on …

Both p53 and its repressor Mdm2 are subject to ubiquitination and proteasomal degradation.
We show that knockdown of the deubiquitinating enzyme USP5 (isopeptidase T) results in …

Selective protein degradation by the ubiquitin-proteasome system (UPS) is involved in all
cellular processes. However, the substrates and specificity of most UPS components are not …

Glucose-dependent regulation of carbon metabolism is a subject of intensive studies. We
have previously shown that the switch from gluconeogenesis to glycolysis is associated with …

Abstract The Saccharomyces cerevisiae Gid-complex is a highly evolutionary conserved
ubiquitin ligase with at least seven protein subunits. Here, we review our knowledge about …

An abundant class of E3 ubiquitin ligases encodes the RING-finger domain. The RING finger
binds to the E2 ubiquitin-conjugating enzyme and brings together both the E2 and substrate …

Ubiquitination is an essential protein modification in eukaryotic cells, which is reversible.
Deubiquitinating enzymes (DUBs) catalyze deubiquitination process to reverse …

Ubiquitination plays a key role in regulating the tumour suppressor p53. It targets p53 for
degradation by the 26S proteasome. The ubiquitin pathway also regulates the activity and …

Ubiquitination is a reversible protein modification that influences various cellular processes
in eukaryotic cells. Deubiquitinating enzymes remove ubiquitin, maintain ubiquitin …