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Nuclear pore glycoprotein p62 (NUP62) is a key structural component of the **nuclear pore complex (NPC)**, a large protein assembly spanning the nuclear envelope that regulates the exchange of macromolecules (e.g., proteins and RNA) between the nucleus and cytoplasm[1][2][3][4][5][6][7]. NUP62 is one of the principal FG-repeat nucleoporins, characterized by multiple phenylalanine-glycine repeats, and localizes to the central channel of the NPC, where it participates in forming the selective barrier and mediates binding to nuclear transport receptors, notably the importin-α/β complex. NUP62 is essential for nucleocytoplasmic transport, as well as for aspects of cell cycle regulation, including centrosome function and spindle orientation during mitosis[2][7]. It assembles into defined subcomplexes (notably with Nup54 and Nup58) and interacts with Nup93 to link central channel and inner ring NPC structures. Although not considered a classical "therapeutic target" such as a receptor or enzyme, altered NUP62 function or expression is linked to autoimmune responses and possibly to some systemic diseases (such as primary biliary cirrhosis and diabetes) via changes in glycosylation or autoantibody generation[1][2]. NUP62 is not currently targeted by any therapeutic drugs, and no mechanism of action of drugs or specific safety concerns related to therapeutic modulation of NUP62 have been described in the literature to date.
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