Golgin-45 (G45) is a coiled-coil protein that transits reversibly between the Golgi and nucleus. In the Golgi, G45 serves as a tether for effectors of a pro-tumorigenic secretory program, but its nuclear role remains unclear. Here, we report that, upon entering the nucleus, G45 functions as a basic leucine zipper transcription factor. From genomic mapping, RNA-sequencing, and functional validation studies, we identify G45-binding sites and show that nuclear G45 can function as a transcriptional activator or repressor, a versatility enabled by phase separation into nuclear bodies enriched in transcriptional co-regulators. In lung cancer models, Golgi-docking reinforces, whereas nuclear translocation opposes, pro-tumorigenic activity of G45. Nuclear G45 incorporates into dimeric transcription factors that silence pro-tumorigenic secreted cargos. Epigenetic events in lung cancer degrade nuclear G45 and sequester G45 in the Golgi, which unleashes malignant secretion. Thus, inter-organelle transitions govern a G45-dependent secretory axis that drives lung cancer progression.
Chao Wu, Abhishek Kumar, Shike Wang, Weina Zhao, Yuanxin Xi, Jing Wang, Abhinav K. Jain, William K. Russell, Hou-fu Guo, Xiaochao Tan, Jonathan M. Kurie
The Editorial Board will only consider comments that are deemed relevant and of interest to readers. The Journal will not post data that have not been subjected to peer review; or a comment that is essentially a reiteration of another comment.