Abstract
Ubiquitylation is a post-translational modification (PTM) that controls various cellular signaling pathways. It is orchestrated by a three-step enzymatic cascade know as the ubiquitin proteasome system (UPS). E3 ligases dictate the specificity to the substrates, primarily leading to proteasome-dependent degradation. Deregulation of the UPS components by various mechanisms contributes to the pathogenesis of cancer. This review focuses on E3 ligase-substrates pairings that are implicated in B-cell malignancies. Understanding the molecular mechanism of specific E3 ubiquitin ligases will present potential opportunities for the development of targeted therapeutic approaches.
Copyright © 2019 Elsevier Inc. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Antineoplastic Agents, Immunological / therapeutic use
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B-Lymphocytes / drug effects
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B-Lymphocytes / immunology
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B-Lymphocytes / pathology
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Bortezomib / therapeutic use
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Humans
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Isoenzymes / genetics
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Isoenzymes / immunology
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Leukemia, B-Cell / drug therapy
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Leukemia, B-Cell / genetics
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Leukemia, B-Cell / immunology*
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Leukemia, B-Cell / pathology
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Molecular Targeted Therapy / methods
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NF-kappa B / genetics
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NF-kappa B / immunology
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Proteasome Endopeptidase Complex / drug effects
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Proteasome Endopeptidase Complex / immunology*
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Proteasome Endopeptidase Complex / metabolism
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Protein Processing, Post-Translational*
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Signal Transduction
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Ubiquitin-Protein Ligases / genetics*
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Ubiquitin-Protein Ligases / immunology
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Ubiquitination
Substances
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Antineoplastic Agents, Immunological
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Isoenzymes
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NF-kappa B
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Bortezomib
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Ubiquitin-Protein Ligases
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Proteasome Endopeptidase Complex