MYG1 is a 3'-5' RNA exonuclease that functions as a critical coordinator of nucleo-mitochondrial crosstalk through selective RNA processing in both cellular compartments 1. The protein exhibits dual subcellular localization, targeting both the nucleolus and mitochondrial matrix via distinct targeting signals 2. In the nucleolus, MYG1 processes pre-ribosomal RNA involved in ribosome assembly and regulates cytoplasmic translation, while in mitochondria, it processes 3'-termini of mito-ribosomal and messenger RNAs to control mitochondrial protein translation 1. Beyond its exonuclease activity, MYG1 demonstrates significant oncogenic properties in cancer progression. In colorectal cancer, nuclear MYG1 promotes glycolysis by recruiting HSP90/GSK3β complexes to stabilize PKM2, which subsequently activates MYC-mediated glycolytic pathways, while mitochondrial MYG1 inhibits oxidative phosphorylation and blocks cytochrome c release to prevent apoptosis 3. Similarly, in breast cancer, MYG1 interacts with HSP90 to activate Wnt/β-catenin and Notch signaling pathways, promoting epithelial-mesenchymal transition and cell cycle progression 4. Clinical relevance includes associations with vitiligo susceptibility through promoter polymorphisms that affect gene expression 56, and potential applications as a biomarker in dilated cardiomyopathy 7. MYG1 also functions as an antiviral factor, limiting mycovirus replication in yeast systems 8.