MAX dimerization protein 1 (MXD1)

MAX dimerization protein 1 (MXD1), also known as MAD or MAD1, is a transcription factor in the MYC/MAX/MAD network, characterized by a basic helix-loop-helix leucine zipper domain (bHLHZip) that mediates DNA binding and dimerization with MAX. MXD1 functions as a transcriptional repressor, antagonizing MYC-driven gene activation by competing for MAX binding and recruiting corepressor complexes such as those containing histone deacetylases. It thus acts as a regulator of cellular proliferation, differentiation, apoptosis, and ribosome biogenesis. MXD1's tumor suppressor function has been implicated in several cancers, and loss or dysregulation of MXD1 can contribute to tumorigenesis, chemoresistance, and altered cytokine expression. No drugs currently target MXD1 directly, but it regulates the molecular response to agents such as imatinib and cisplatin through repression of driver genes and interaction with major signaling pathways.

Other names

MADMAD1Max dimerizer 1Protein MADBHLHC58Max dimerization protein 1max-binding proteinantagonizer of myc transcriptional activity

Not directly drug-targeted; mechanisms described refer to gene expression modulation, e.g.: - Repression of BCR-ABL1 (modulates imatinib sensitivity in CML) - Repression of PTEN gene expression (modulates cisplatin sensitivity in osteosarcoma)