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Nuclear pore membrane glycoprotein 210 (NUP210) is a large single-pass transmembrane glycoprotein essential for the assembly, spacing, and structural integrity of the nuclear pore complex (NPC) in eukaryotic cells[4][2]. The majority of NUP210's mass lies in a luminal domain situated within the perinuclear space, with only a small C-terminal tail facing the cytoplasm[1]. While initially thought to be a structural component required for nuclear pore complex biogenesis, recent data indicate that NUP210 is dispensable for basal NPC assembly but is instead critical for the differentiation of certain cell types, including muscle and neuronal cells[1]. NUP210 exerts antiapoptotic activity during differentiation by maintaining nuclear envelope/ER homeostasis and mitigating ER stress responses[1]. It also plays a role in chromatin tethering, mechanosensory signal integration, and metastatic capacity in cancer cells, particularly estrogen receptor–positive (ER+) breast cancer, where its depletion suppresses metastasis[3]. Pathologically, NUP210 is recognized by autoantibodies in primary biliary cholangitis, and its aberrant or elevated expression is associated with disease severity in liver disease and some cancers[2][3][4]. No approved drugs are known to specifically target NUP210, and its key clinical significance presently lies in its biomarker roles for autoimmunity and cancer prognosis.
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