Nuclear prelamin A recognition factor (NARF)

Nuclear prelamin A recognition factor (NARF) is a nuclear protein that specifically binds to the prenylated C-terminal tail domain of prelamin A, a precursor of lamin A. Its binding depends on the farnesylation status of prelamin A, making it an example of prenyl-dependent protein-protein interaction. NARF partially colocalizes with the nuclear lamina and may be part of a prelamin A endoprotease complex involved in lamin A maturation. Recent studies have uncovered a role for NARF as a transcriptional coactivator in hypoxic breast cancer cells, where it enhances stemness and metastatic features by epigenetically upregulating pluripotency factor genes. Additionally, NARF has been linked to mitochondrial dysfunction and iron metabolism dysregulation in neurological disease contexts such as multiple sclerosis. Structurally, NARF shows limited sequence similarity to iron-only bacterial hydrogenases, and several transcript variants exist due to alternative splicing and RNA editing

Other names

IOP2FLJ10067DKFZp434G0420Iron-only hydrogenase-like protein 2prenyl-dependent prelamin A binding protein