STAT3 and lung cancer: Investigators have found that myristoylation of a glycine residue at the N-terminus of EZH2 mediates its phase separation and enables the signal transducer and activator of transcription 3 (STAT3) recruitment, and that the enhanced EZH2-STAT3 interaction increases the activation and transcriptional activity of STAT3 and its downstream effectors, ultimately leading to the accelerated proliferation of lung cancer cells[20].