Abstract
Nuclear pore complexes (NPCs) regulate the entry and exit of molecules from the cell nucleus. Small molecules pass through NPCs by diffusion while large molecules enter and exit the nucleus by karyopherins, which serve as transport factors. Exportin-1 (XPO1) is a protein that is an important member of the karyopherin family and carries macromolecules from the nucleus to the cytoplasm. XPO1 is responsible for nuclear-cytoplasmic transport of protein, ribosomal RNA and certain required mRNAs for ribosomal biogenesis. Furthermore, XPO1-mediated nuclear export is associated with various types of disease, such as cancer, inflammation and viral infection. The key role of XPO1 in carcinogenesis and its potential as a therapeutic target has been demonstrated by previous studies. Clinical use of novel developed generation-specific XPO1 inhibitors and their combination with other agents to block XPO1-mediated nuclear export are a promising new treatment strategy. The aim of the present study was to explain the working mechanism of XPO1 and inhibitors that block XPO1-mediated nuclear export.