Ubiquitination of Immune System and Cancer Therapy
Authors:
- 16 November 2024
- book chapter
- Published by Springer Nature
- Vol. 1466, 35-45
Abstract
Ubiquitination is a post-translational modification mechanism which regulates a variety of signaling pathways and crucial biological processes. It has long been known that ubiquitination regulates the fundamental cellular processes through the induction of proteasomal degradation of target proteins. Meanwhile, the nondegradative types of polyubiquitination modification have been appreciated as important regulatory machinery by modulating the activity or subcellular localization of key signaling proteins. The function of ubiquitination plays an important role in immune responses, which helps to maintain the stability of the internal environment and to control over protein stability and function and are thus critical for the regulation of both innate and adaptive immunity. Furthermore, ubiquitination also regulates both tumor-suppressing and tumor-promoting pathways in cancer. In this review, we will discuss recent progress regarding how ubiquitination regulates immune responses, focusing on Toll-like receptors signaling in innate immunity, T cell activation, TCR signaling, and tumor immunotherapy.Keywords
This publication has 102 references indexed in Scilit:
- Constitutive Endocytosis and Degradation of the Pre-T Cell ReceptorJournal of Experimental Medicine, 2002
- Predominant Role of T Cell Receptor (TCR)-α Chain in Forming Preimmune TCR Repertoire Revealed by Clonal TCR Reconstitution SystemJournal of Experimental Medicine, 2002
- Negative regulation of Lck by Cbl ubiquitin ligaseProceedings of the National Academy of Sciences, 2002
- Mapping the Zap-70 phosphorylation sites on LAT (linker for activation of T cells) required for recruitment and activation of signalling proteins in T cellsBiochemical Journal, 2001
- LAT, the Linker for Activation of T Cells: A Bridge Between T Cell-Specific and General Signaling PathwaysScience's STKE, 2000
- Engagement of the Pd-1 Immunoinhibitory Receptor by a Novel B7 Family Member Leads to Negative Regulation of Lymphocyte ActivationJournal of Experimental Medicine, 2000
- Ras regulation and function in lymphocytesCurrent Opinion in Immunology, 2000
- The F-box protein β-TrCP associates with phosphorylated β-catenin and regulates its activity in the cellCurrent Biology, 1999
- Involvement of p21ras activation in T cell CD69 expressionEuropean Journal of Immunology, 1994
- Induced expression of PD‐1, a novel member of the immunoglobulin gene superfamily, upon programmed cell death.The EMBO Journal, 1992