Lung cancer is first cause of cancer-related death worldwide, followed by colorectal cancer (CRC). There is an unmet need to explore novel cancer-specific targets involved in malignant phenotypes to improve current therapy. The objective of this thesis is to explore the role of peptidyl-prolyl-cis-trans-isomerase (PPIase) FK506-binding protein 10 (FKBP10) in lung and colorectal cancers. Herein, we report that FKBP10 is specifically expressed in human lung and colorectal cancer lesions, and absent in healthy lung parenchyma and colonic mucosa. Furthermore, FKBP10 expression negatively correlates with survival of lung cancer patients, and its expression is positively related to tumor grade and cancer recurrence of CRC patients. By investigating the therapeutic potential of targeting FKBP10 in a KRAS-driven lung tumorigenesis mouse model, we show that while in mice with intact FKBP10, the tumor volume continues to increase, FKBP10 ablation greatly reduces tumor burden in these animals. Our results from gain- and loss-of-function in vitro assays indicates that FKBP10 boosts cancer growth and stemness of lung and colorectal cancer cells via its PPIase activity. Further investigation revealed that FKBP10 interacts with ribosomes, and its silencing leads to a significant reduction of protein translation. Mechanistically, we uncovered that FKBP10 downregulation leads to a reduction of translation elongation at the beginning of open reading frames, in particular upon the insertion of proline residues, therefore, playing a role in translational reprogramming of cancer cells. Collectively, this project unveiled FKBP10 as a cancer-selective molecule exerting an important role in the regulation of protein translation, hence supporting cancer growth and stemness. Inhibiting FKBP10 may show promising therapeutic opportunity as a personalized medicine to increase the efficacy and safety of therapies against lung and colorectal cancers.