MRPL13 is a mitochondrial ribosomal protein that serves as a structural component of the mitochondrial large ribosomal subunit and plays a critical role in mitochondrial protein synthesis and oxidative phosphorylation (OXPHOS) regulation 1. The protein functions in translating OXPHOS complex subunits, which are essential for mitochondrial ATP production and cellular energy metabolism 1. Mechanistically, MRPL13 interacts with SLC25A6 and promotes its degradation via K48-linked ubiquitination, thereby inhibiting mitochondrial permeability transition pore (mPTP) opening and preventing cytochrome c release 1. This mechanism enhances mitochondrial function and prevents cell death. Clinically, MRPL13 is significantly overexpressed across multiple cancer types including ovarian, lung adenocarcinoma, gastric, breast, and hepatocellular carcinoma 12345. High MRPL13 expression correlates with poor prognosis, promotes tumor cell proliferation, migration, invasion, and metastasis while inhibiting apoptosis 234. The protein appears to promote cancer progression by inhibiting p53 signaling and facilitating cell cycle progression 3. Conversely, MRPL13 deficiency impairs mitochondrial function, reduces OXPHOS capacity, and can be mediated by lactate exposure in hepatoma cells 6, suggesting its potential as both a diagnostic biomarker and therapeutic target.