Related Experiment Video
Updated: Jul 10, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
Protein-protein interactions regulate Ubl conjugation
Puck Knipscheer1, Titia K Sixma
1Division of Molecular Carcinogenesis, The Netherlands Cancer Institute and Center for Biomedical Genetics, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands.
Abstract:
The ubiquitin-like proteins (Ubls) can be covalently linked to target proteins to provide a critical signal in diverse cellular processes. Members of the Ubl family include ubiquitin itself and a growing number of homologs such as SUMO, Nedd8, ISG15 and Atg8. The enzymatic mechanism of Ubl conjugation involves an E1, E2, E3 cascade of enzymes that is well conserved between the Ubls. In the past two years, novel structural details of Ubl conjugation were uncovered through analysis of protein-protein complexes. This has given insight in activation of E1, the role of the target lysine in E2-dependent catalysis, the role of noncovalent Ubl binding in Ubl chain formation and the importance of dimerization of Ring-type E3 ligases.
Related Concept Videos
Protein-protein Interfaces
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Regulated Protein Degradation
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Protein Networks
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

