The Ubiquitin Code

2012/05/22 by David Komander, Michael Rape, Michael Rapé · 32 citations
Biochemistry, Genetics and Molecular Biology · Medicine · #Ubiquitin and proteasome pathways #Autophagy in Disease and Therapy #Cancer-related Molecular Pathways

paper · doi:10.1146/annurev-biochem-060310-170328

Abstract

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.

Cited by

• Ubiquitin Ligases: Structure, Function, and Regulation
• Driving E3 Ligase Substrate Specificity for Targeted Protein Degradation: Lessons from Nature and the Laboratory
• Proteostasis regulation by the ubiquitin system
• Harnessing the ubiquitin code to respond to environmental cues
• Interplay between ubiquitination and ADP-ribosylation and the case of dual modification ADPr-Ub
• The importance of UBQLN2 ubiquitylation for its turnover and localization
• Decoding Chromatin Ubiquitylation: A Chemical Biology Perspective
• USP1/UAF1 targets polyubiquitinated PCNA with an exo-cleavage mechanism that can temporarily enrich for monoubiquitinated PCNA
• High air humidity dampens salicylic acid pathway and NPR1 function to promote plant disease
• Molecular Phylogeny of the SELMA Translocation Machinery Recounts the Evolution of Complex Photosynthetic Eukaryotes
• The ubiquitin code of receptor kinases in plants
• Mechanisms and regulation of substrate degradation by the 26S proteasome
• The <scp>BioGRID</scp> database: A comprehensive biomedical resource of curated protein, genetic, and chemical interactions
• Tuning ubiquitin transfer by RING E3 ubiquitin ligases through the linchpin residue
• Meta‐analysis fails to show any correlation between protein abundance and ubiquitination changes
• The Ubiquitin Script: writing protein fates in chains
• Recent Advances in Ubiquitin Signals Regulating Plant Membrane Trafficking
• STING induces HOIP-mediated synthesis of M1 ubiquitin chains to stimulate NF-κB signaling
• Two sides of a coin: Physiological significance and molecular mechanisms for damage-induced mitochondrial localization of PINK1 and Parkin
• Bendless-mediated K63 ubiquitination modulates cellular signalling to regulate Drosophila hematopoiesis
• Targeting NF-κB pathway for the therapy of diseases: mechanism and clinical study
• PROTAC targeted protein degraders: the past is prologue
• The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy
• The Deubiquitinase OTULIN Is an Essential Negative Regulator of Inflammation and Autoimmunity
• Physiological Functions of the Ubiquitin Ligases Nedd4-1 and Nedd4-2
• Conformational and functional characterization of artificially conjugated non-canonical ubiquitin dimers
• Sequence rules for a long SPOP-binding degron required for protein ubiquitylation
• Holding RIPK1 on the Ubiquitin Leash in TNFR1 Signaling
• Advancing the Exploration of the Ubiquitin‐like Protein FUBI with Synthetic Chemical Tools
• Deciphering the Molecular Signals of PINK1/Parkin Mitophagy
• Muskelin is a substrate adaptor of the highly regulated Drosophila embryonic CTLH E3 ligase
• Ubiquitin signatures on aggregating proteins in neurodegeneration

Related

• The Ubiquitin Script: writing protein fates in chains
• Harnessing the ubiquitin code to respond to environmental cues
• THE UBIQUITIN SYSTEM
• UBIQUITIN-DEPENDENT REGULATION OF THE SYNAPSE
• Proteostasis regulation by the ubiquitin system