Cited by 136Ubiquitin and proteasome pathwaysCancer-related Molecular PathwaysCancer-related gene regulation

A Comprehensive Guide to the MAGE Family of Ubiquitin Ligases

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Lee, Anna K., Potts, Patrick Ryan·2017·Journal of Molecular Biology

Abstract

Melanoma antigen (MAGE) genes are conserved in all eukaryotes and encode for proteins sharing a common MAGE homology domain. Although only a single MAGE gene exists in lower eukaryotes, the MAGE family rapidly expanded in eutherians and consists of more than 50 highly conserved genes in humans. A subset of MAGEs initially garnered interest as cancer biomarkers and immunotherapeutic targets due to their antigenic properties and unique expression pattern that is primary restricted to germ cells and aberrantly reactivated in various cancers. However, further investigation revealed that MAGEs not only drive tumorigenesis but also regulate pathways essential for diverse cellular and developmental processes. Therefore, MAGEs are implicated in a broad range of diseases including neurodevelopmental, renal, and lung disorders, and cancer. Recent biochemical and biophysical studies indicate that MAGEs assemble with E3 RING ubiquitin ligases to form MAGE-RING ligases (MRLs) and act as regulators of ubiquitination by modulating ligase activity, substrate specification, and subcellular localization. Here, we present a comprehensive guide to MAGEs highlighting the molecular mechanisms of MRLs and their physiological roles in germ cell and neural development, oncogenic functions in cancer, and potential as therapeutic targets in disease.

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Crossref · 10.1016/j.jmb.2017.03.005

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  • The MAGE family of ubiquitin E3 ligases, often called MAGE-RING ligases (MRLs), comprise proteins that serve as substrate-recruitment modules for other RING E3 ligases, adding to and/or altering the substrate specificity of their co-E3 ligases.

    “An example of such a family of ligases are the MAGE (melanoma antigen genes) family of ubiquitin E3 ligases, often referred to as the MAGE-RING ligases (MRLs), which comprise proteins that serve as substrate-recruitment modules for other RING E3 ligases156,157, adding to and/or altering the substrate specificity of their co-E3 ligases (reviewed elsewhere155,158).”

    From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [158]

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Authors
Lee, A. K., & Potts, P. R.
Affiliations
St. Jude Children's Research Hospital (US)
Corresponding author
Potts, Patrick Ryan
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
2017-04
Volume
429
Issue
8
Pages
1114-1142
ISSN
0022-2836 (ISSN-L)
OpenAlex
W2592245646
Cited by
136
References
229
Citations by year
2026: 12 · 2025: 17 · 2024: 10 · 2023: 11 · 2022: 18 · 2021: 16 · 2020: 24 · 2019: 11 · 2018: 12 · 2017: 5
FWCI
1.33
Type
journal article
Language
en
Open access
Locations
  • Journal of Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institute of General Medical Sciences (R01GM111332)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
Keywords
E3 ubiquitin ligase, ubiquitination, germ cell development, neural development, carcinogenesis, tumor markers, immunotherapy targets, therapeutic target
MeSH terms
Antigens, Neoplasm, Bartter Syndrome, Chromosome Mapping, Multigene Family, Humans, Immunotherapy, Neoplasms, Prader-Willi Syndrome, Gene Expression Regulation, Developmental, Evolution, Molecular, Ubiquitin-Protein Ligases, Ubiquitination, Melanoma-Specific Antigens

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