Ubiquitin and intracellular protein degradation.
In eukaryotes, the ubiquitin-dependent protoelytic pathway is one of the major routes by which intracellular proteins are selectively destroyed. Recent work has shown that conjugation of ubiquitin to substrate proteins is mediated by a remarkably diverse array of enzymes. Proteolytic targeting may also be regulated at steps between ubiquitination of the substrate and its degradation to peptides by the multisubunit 26S protease. The complexity of the ubiquitin system suggests a central role for protein turnover in eukaryotic cell regulation.
Hochstrasser
M
M
Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637.
D000818:Animals; D006801:Humans; D008025:Ligases / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex; D011506:Proteins / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology; D014452:Ubiquitins / Q000502:physiology*
D011506:Proteins; D014452:Ubiquitins; D010447:Peptide Hydrolases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease; D008025:Ligases