E3 ubiquitin ligases in B-cell malignancies

Cell Immunol. 2019 Jun:340:103905. doi: 10.1016/j.cellimm.2019.02.004. Epub 2019 Feb 26.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Antineoplastic Agents, Immunological / therapeutic use
  • B-Lymphocytes / drug effects
  • B-Lymphocytes / immunology
  • B-Lymphocytes / pathology
  • Bortezomib / therapeutic use
  • Humans
  • Isoenzymes / genetics
  • Isoenzymes / immunology
  • Leukemia, B-Cell / drug therapy
  • Leukemia, B-Cell / genetics
  • Leukemia, B-Cell / immunology*
  • Leukemia, B-Cell / pathology
  • Molecular Targeted Therapy / methods
  • NF-kappa B / genetics
  • NF-kappa B / immunology
  • Proteasome Endopeptidase Complex / drug effects
  • Proteasome Endopeptidase Complex / immunology*
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Processing, Post-Translational*
  • Signal Transduction
  • Ubiquitin-Protein Ligases / genetics*
  • Ubiquitin-Protein Ligases / immunology
  • Ubiquitination

Substances

  • Antineoplastic Agents, Immunological
  • Isoenzymes
  • NF-kappa B
  • Bortezomib
  • Ubiquitin-Protein Ligases
  • Proteasome Endopeptidase Complex