title: When MAGE meets RING: insights into biological functions of MAGE proteins.
abstract: The melanoma antigen (MAGE) family proteins are well known as tumor-specific antigens and comprise more than 60 genes, which share a conserved MAGE homology domain (MHD). Type I MAGEs are highly expressed cancer antigens, and they play an important role in tumorigenesis and cancer cell survival. Recently, several MAGE proteins were identified to interact with RING domain proteins, including a sub-family of E3 ubiquitin ligases. The binding mode between MAGEs and RING proteins was investigated and one important structure of these MAGE-RING complexes was solved: the MAGE-G1-NSE1 complex. Structural and biochemical studies indicated that MAGE proteins could adjust the E3 ubiquitin ligase activity of its cognate RING partner both in vitro and in vivo. However, the underlying mechanism was not fully understood. Here, we review these exciting advances in the studies on MAGE family, suggest potential mechanisms by which MAGEs activate the E3 activity of their binding RING proteins and highlight the anticancer potential of this family proteins.
authors.affiliation: MOE Key Laboratory of Bioinformatics, Tsinghua University, Beijing, 100084, China.
authors.forename: Yue
authors.initials: Y
authors.lastname: Feng
authors.forename: Jinlan
authors.initials: J
authors.lastname: Gao
authors.forename: Maojun
authors.initials: M
authors.lastname: Yang
mesh_terms: D000818:Animals; D006801:Humans; D058950:Melanoma-Specific Antigens / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D058950:Melanoma-Specific Antigens