{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTransportin‐1 (TNPO1), also known as karyopherin‐β2, is a pivotal nuclear import receptor that recognizes non‐classical proline–tyrosine nuclear localization signals (PY‐NLSs) and related motifs on a wide array of cargo proteins. Through direct binding via multiple, often regulated, interaction epitopes, TNPO1 mediates the nuclear import of several RNA‐binding proteins and transcription factors – including FUS, ADAR1, heterogeneous nuclear ribonucleoproteins, FOXO, and Huntingtin – thereby ensuring their correct subcellular localization and function. Detailed structural and biochemical analyses reveal that TNPO1’s engagement with these cargos is modulated by post‐translational modifications such as arginine methylation and acetylation; disruption of these interactions results in altered nuclear targeting, aberrant phase transitions (for example, increased stress granule formation), and is associated with neurodegenerative conditions such as familial amyotrophic lateral sclerosis and frontotemporal lobar degeneration."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its classical nuclear‐import role, TNPO1 functions as a multifaceted regulator in viral infection and cellular stress responses. It directly engages with viral proteins and capsid components—such as motifs present in HIV‐1 capsid proteins, influenza A matrix protein, and oncoproteins of human papillomaviruses—to trigger critical events like uncoating and subsequent nuclear import. Moreover, TNPO1’s activity can itself be modulated by competing interactions with arginine‐rich poly‐dipeptides or by changes in microRNA expression (for example, miR‐128 targeting its mRNA), thereby influencing not only viral replication cycles but also retrotransposition events."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTNPO1 also serves specialized and context‐dependent transport roles beyond conventional nuclear import. It facilitates the targeting of proteins to specific subcellular compartments such as the primary cilium—as observed for the retinitis pigmentosa 2 protein and Arl13b—and contributes to the nuclear entry or shuttling of key regulatory factors including fibroblast growth factor‐2 (FGF2), PQBP1, BAP1, and ARID1B. These processes link TNPO1 function to the regulation of circadian rhythms, autophagy, and oncogenic signaling cascades, and are underpinned by extensive structural remodeling within TNPO1 during cargo recognition and release."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Jutta Fritz, Alexander Strehblow, Andreas Taschner, et al. 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