NMT1 (N-myristoyltransferase 1) is a cytoplasmic enzyme that catalyzes the cotranslational transfer of myristic acid to N-terminal glycine residues of nascent proteins, and can also mediate lysine myristoylation 1. NMT1 exchanges with methionine aminopeptidases at the ribosomal tunnel exit, forming an active complex with nascent polypeptide-associated complex to access newly synthesized substrates 1. Mechanistically, myristoylation regulates protein membrane localization, trafficking, and stability; for example, NMT1-mediated myristoylation of TMEM106B promotes its lysosomal degradation and affects cellular trafficking 2, while myristoylation of ICAM-1 prevents its ubiquitin-mediated degradation 3. NMT1 dysregulation is associated with multiple malignancies, with elevated expression observed in colon, lung, and breast tumors correlating with poor survival 4. In cancer, NMT1 promotes tumorigenesis through diverse mechanisms: facilitating proliferation via VILIP3-NFκB/Bcl-2 signaling in hepatocellular carcinoma 5, enhancing PD-L1 membrane localization under hypoxia 6, and supporting oxidative phosphorylation through mitochondrial complex I assembly 7. NMT1 inhibition is therapeutically relevant, with NMT inhibitor zelenirstat in phase 1/2a trials for lymphoma and solid tumors 7. Additionally, NMT1 deficiency impairs immune cell function in rheumatoid arthritis 8.