MAX dimerization protein MGA (MGA)

MAX dimerization protein MGA (commonly abbreviated as MGA) is a dual-specificity transcription factor central to the regulation of MYC-dependent gene expression. MGA contains two functional DNA-binding domains: a basic helix-loop-helix leucine zipper (bHLHZip) and a T-box domain[1][3]. MGA exerts its regulatory effects by heterodimerizing with MAX, enabling it to either repress or activate transcription at target gene loci containing E-box or Brachyury binding sites. MGA counteracts MYC-driven oncogenic programs by repressing MYC-target genes and controlling cell fate, proliferation, and the cell cycle[1][3]. Loss or inactivation of MGA contributes to various cancers, such as lung adenocarcinoma and hematopoietic malignancies, by unleashing unchecked MYC activity. MGA also modulates the tumor immune microenvironment, and its genetic loss can enhance antitumor immune responses[1]. MGA is part of the T-box gene family and serves predominantly as a transcriptional regulator, with influences on cell differentiation and proliferation critical in development and disease[2][3].\n\nNote: MGA sometimes refers to Mammaglobin A in oncology diagnostics, particularly as a marker for breast cancer, but this is a distinct protein and should not be conflated with MAX dimerization protein MGA[1].

Other names

MAX gene-associated proteinKIAA0518MAD5MXD5FLJ12634POF26MGA proteinMAX dimerization protein 5