Ubiquitination and deubiquitination as critical modulators of NSCLC tumorigenesis and drug resistance

Ubiquitination and deubiquitination are biological mechanisms that including the addition and removal ubiquitin molecules from proteins, which are associated with NSCLC. NSCLC is the most common kind of lung cancer, and treatment resistance and cancer development are linked to these alterations. Ubiquitination incorporates proteins by a particular enzyme class, and deubiquitination removes ubiquitins. In NSCLC, this modification is detrimental to cellular function and affects tumorigenesis, apoptosis, and signaling pathways. Conversely, deubiquitination refers to the process through which the ubiquitins are removed from the proteins so that they can perform their functions properly. These processes can be considered therapeutic in some sense, as regulating both can result in an effective therapy for NSCLC. Many studies have been carried out to find potential areas where further drug research could be focused. This study examines the functions of ubiquitination and deubiquitination in NSCLC pathogenesis and resistance, focusing on their mechanisms, consequences, and therapeutic possibilities.