Max-like protein X (MLX)

Max-like protein X (MLX) is a basic helix-loop-helix leucine zipper (bHLH-Zip) transcription factor that acts as a key dimerization partner for members of the MYC/MAX/MLX network, particularly with proteins such as MondoA and ChREBP[2][4][6]. MLX is essential for coupling metabolic signals (notably glucose and lipid-related cues) to nuclear gene expression, thereby regulating processes such as glycolysis and de novo lipogenesis. Mechanistically, MLX forms heterodimers or higher-order complexes that bind to carbohydrate response elements (ChoREs) and modulate transcription of target genes in response to metabolic status[2][5]. MLX is implicated in cancer biology, as it is essential for the metabolic adaptations of MYC-driven tumors, and in metabolic diseases, including fatty liver and Takayasu arteritis, due to its role in hepatic and systemic energy metabolism[2][6]. No FDA-approved drugs directly target MLX, but it remains a subject of therapeutic interest, especially for metabolic cancer vulnerabilities and metabolic disease modulation[1][2][6].

Other names

Max-like protein XMLXBHLHD13TCFL4bHLHd13MAD7MXD7Class D basic helix-loop-helix protein 13Max-like bHLHZip proteinProtein BigMaxTranscription factor-like protein 4BigMax proteinMAX-like bHLHZIP proteinMAX dimerization proteinmax-like protein X

Transcriptional co-activation or repression via heterodimerization with nutrient-sensing transcription factors such as MondoA and ChREBP, which in turn regulate metabolic gene expression[2][4][5].