Related Experiment Video
Updated: Apr 28, 2026

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
Ubiquitylation in innate and adaptive immunity
1Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
Abstract:
Protein ubiquitylation has emerged as a key mechanism that regulates immune responses. Much like phosphorylation, ubiquitylation is a reversible covalent modification that regulates the stability, activity and localization of target proteins. As such, ubiquitylation regulates the development of the immune system and many phases of the immune response, including its initiation, propagation and termination. Recent work has shown that several ubiquitin ligases help to prevent the immune system from attacking self tissues. The dysfunction of several ubiquitin ligases has been linked to autoimmune diseases.
Related Concept Videos
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...
Regulation of the Unfolded Protein Response
Introduction to Innate and Adaptive Immunity
Innate immunity is the body's natural, nonspecific defense system that acts quickly to protect against pathogens. It incorporates physical barriers like skin and mucous membranes and cellular elements such as phagocytes and natural killer cells. This part of our immune system provides an immediate,...
Antigens Involved in Adaptive Immunity
Complete Antigens
Complete antigens possess both immunogenicity and...
B Cell Activation and Differentiation
When naive B cells encounter a specific antigen that can bind to the B cell receptor (BCR) on their surface, they undergo sensitization to respond to the antigen's presence. Sensitization begins with...

