TOMM34 (translocase of outer mitochondrial membrane 34) is a cytosolic chaperone-like protein that facilitates mitochondrial protein import by maintaining precursor proteins in an unfolded, import-compatible state 1. The protein contains two tetratricopeptide repeat (TPR) domains that enable simultaneous binding to both HSP70 and HSP90, forming a tripartite Hsp70-TOMM34-Hsp90 chaperone complex 2. TOMM34 function is regulated by protein kinase A-mediated phosphorylation at Ser93 and Ser160, which promotes binding to 14-3-3 adaptor proteins and modulates HSP70 interactions 3. Expression is primarily controlled by nuclear respiratory factor-1 (NRF-1), reflecting its role in mitochondrial biogenesis 1. TOMM34 is frequently overexpressed in multiple cancers, including colorectal, ovarian, and oral squamous cell carcinomas, where it promotes cell proliferation, migration, and invasion while maintaining mitochondrial integrity and reducing oxidative stress 456. In hepatocellular carcinoma, TOMM34 interacts with ATP5B to preserve mitochondrial ATP synthesis during metabolic stress 7. Additionally, TOMM34 contributes to antiviral immunity by facilitating NF-κB activation through TRAF6-mediated NEMO ubiquitination, playing a role in hyperinflammation during severe COVID-19 and influenza infections 8.