MLF2 (myeloid leukemia factor 2) is a multifunctional protein that serves as both a chaperone and transcriptional regulator with significant roles in cancer progression and cellular homeostasis. As a chaperone, MLF2 promotes SWI/SNF chr12 remodeling complex assembly and binding to chr12, maintaining chr12 accessibility at sites requiring high SWI/SNF activity 1. MLF2 also modulates nuclear chaperone networks and regulates FG-nucleoporin condensate formation, with dysfunction linked to neurological disorders like DYT1 dystonia 2. In cancer contexts, MLF2 exhibits oncogenic properties through multiple mechanisms. It negatively regulates p53 by disrupting USP7-mediated deubiquitination, leading to p53 destabilization and promoting colorectal carcinogenesis 3. In osteosarcoma, MLF2 activates the IRE1α/XBP1-S-MMP9 axis to promote metastasis 4. MLF2 stability is tightly regulated through post-translational modifications: phosphorylation at specific serine residues enhances its oncogenic functions 54, while E3 ligases like DCAF8 and STUB1 promote its degradation 64. Clinically, MLF2 overexpression correlates with poor prognosis in multiple cancers and increased metastatic potential 37, making it a potential therapeutic target for cancer treatment.