{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSUN1 is a conserved integral protein of the inner nuclear membrane that plays a central architectural role in the assembly of the LINC (Linker of Nucleoskeleton and Cytoskeleton) complex. It binds directly to nuclear envelope‐anchored nesprins and other inner nuclear membrane partners to physically “bridge” the nuclear interior with the cytoskeleton, thereby facilitating nuclear anchorage and migration. Early genetic and biochemical studies in model organisms and mammalian cells underscore its conserved function in nuclear positioning, where mutations in its homolog (UNC-84) disrupt nuclear migration and anchorage."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its structural role, SUN1 modulates diverse aspects of nuclear dynamics. It contributes to nuclear envelope remodeling during mitosis—promoting de-condensation, regulating nuclear pore complex (NPC) assembly and distribution, and influencing interactions with lamins and chromatin. This protein assists in proper NPC localization and even plays a role in optimizing mRNA export by directly binding export factors and nucleoporins. Its interaction with various binding partners is critical for maintaining nuclear integrity during cell division and for orchestrating the re‐establishment of nuclear architecture post-mitosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulation of SUN1 underlies a range of human pathologies. Abnormal accumulation or mislocalization of SUN1 contributes to various laminopathies—including Emery–Dreifuss muscular dystrophy, Hutchinson–Gilford progeria, and other disorders linked to defects in nuclear envelope structure. In these disease contexts, altered SUN1 levels disturb nuclear-cytoskeletal coupling and compromise the stability of the nuclear envelope. Furthermore, aberrant interactions with its binding partners lead to impaired nuclear transport, defective chromatin organization, and consequent cellular stress responses, thereby amplifying disease phenotypes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, SUN1 is emerging as a multifaceted regulator in specialized cellular processes. 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