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Updated: Apr 18, 2026

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
Regulation of T cell receptor complex-mediated signaling by ubiquitin and ubiquitin-like modifications
Samantha F Friend1, Francina Deason-Towne2, Lisa K Peterson1
1Department of Pediatrics, University of Colorado School of Medicine Aurora, CO 80045, USA ; Integrated Department of Immunology, University of Colorado School of Medicine and National Jewish Health Denver, CO 80206, USA.
Abstract:
Post-translational protein modifications are a dynamic method of regulating protein function in response to environmental signals. As with any cellular process, T cell receptor (TCR) complex-mediated signaling is highly regulated, since the strength and duration of TCR-generated signals governs T cell development and activation. While regulation of TCR complex-mediated signaling by phosphorylation has been well studied, regulation by ubiquitin and ubiquitin-like modifiers is still an emerging area of investigation. This review will examine how ubiquitin, E3 ubiquitin ligases, and other ubiquitin-like modifications such as SUMO and NEDD8 regulate TCR complex-mediated signaling.
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