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Ubiquitin ligases and the immuneresponse
Author(s): Liu YC
Source: ANNUAL REVIEW OF IMMUNOLOGY    Volume: 22    Pages: 81-127    Published: 2004  
Times Cited: 111     References: 313     
Abstract: Ubiquitin (Ub)-protein conjugation represents a novel means of post-transcriptional modification in a proteolysis-dependent or -independent manner. E3 Ub ligases play a key role in governing the cascade of Ub transfer reactions by recognizing and catalyzing Ub conjugation to specific protein substrates. The E3s, which can be generally classified into HECT-type and RING-type families, are involved in the regulation of many aspects of the immune system, including the development, activation, and differentiation of lymphocytes, T cell-tolerance induction, antigen presentation, immune evasion, and virus budding. E3-promoted ubiquitination affects a wide array of biological processes, such as receptor downmodulation, signal transduction, protein processing or translocation, protein-protein interaction, and gene transcription, in addition to proteasome-mediated degradation. Deficiency or mutation of some of the E3s like Cbl, Cbl-b, or Itch, causes abnormal immune responses such as autoimmunity, malignancy, and inflammation. This review discusses our current understanding of E3 Ub ligases in both innate and adaptive immunity. Such knowledge may facilitate the development of novel therapeutic approaches for immunological diseases.
Document Type: Review
Language: English
Reprint Address: Liu, YC (reprint author), La Jolla Inst Allergy & Immunol, Div Cell Biol, San Diego, CA 92121 USA
Addresses:
1. La Jolla Inst Allergy & Immunol, Div Cell Biol, San Diego, CA 92121 USA
Publisher: ANNUAL REVIEWS, 4139 EL CAMINO WAY, PO BOX 10139, PALO ALTO, CA 94303-0139 USA
Subject Category: Immunology
IDS Number: 823HP
ISSN: 0732-0582
DOI: 10.1146/annurev.immunol.22.012703.104813
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