2012/05/22 by David Komander, Michael Rape, Michael Rapé · 3,702 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Medicine · #Autophagy in Disease and Therapy #Biochemistry #Biology #Cancer-related Molecular Pathways #Cell biology #Chemistry #Computational biology #Deubiquitinating enzyme #Function (biology) #Moiety #Stereochemistry #Ubiquitin #Ubiquitin and proteasome pathways #Ubiquitin ligase #Ubiquitin-Protein Ligases
paper · doi:10.1146/annurev-biochem-060310-170328
published in Annual Review of Biochemistry 81(1), 203-229 (Annual Reviews)
openalex publication_date 2012/05/22 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/05
The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds. Reminiscent of a code, the various ubiquitin modifications adopt distinct conformations and lead to different outcomes in cells. Here, we discuss the structure, assembly, and function of this ubiquitin code.