ZMPSTE24 is a transmembrane zinc metalloprotease located on the inner nuclear membrane that catalytically processes prelamin A by proteolytically removing its C-terminal three residues after farnesylation 1. This processing is critical for generating mature lamin A, a nuclear scaffold protein essential for nuclear envelope integrity 2. Beyond its protease function, ZMPSTE24 clears clogged translocons on the endoplasmic reticulum 1. The enzyme also exhibits antiviral activity independently of its proteolytic function by restricting enveloped RNA and DNA viruses including influenza A, Zika, and Ebola through modulation of the IFITM antiviral pathway and membrane fluidity 34. Mutations in ZMPSTE24 cause premature aging diseases including Hutchinson-Gilford Progeria Syndrome (HGPS), mandibuloacral dysplasia-type B, and restrictive dermopathy, characterized by defective prelamin A processing and accumulation 25. In ZMPSTE24-deficient models, prelamin A accumulation triggers cellular senescence in postmitotic muscle through mtDNA release, cGAS-STING activation, and SASP factor secretion 6. Lonafarnib, a farnesyltransferase inhibitor, was FDA-approved to reduce mortality in HGPS and processing-deficient progeroid laminopathies by preventing pathogenic protein farnesylation 7.