The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Identity is verified. The requested target is human SUN1 (Sad1 and UNC84 domain-containing protein 1; aliases KIAA0810 and UNC84A), UniProt O94901—not a similarly named plant, fungal, or non-human SUN protein. Literature explicitly associates O94901 with human SUN1 isoforms and identifies mammalian SUN1/UNC84A as a widely expressed, type-II integral protein of the inner nuclear membrane (INM). Its reported topology and SUN/coiled-coil architecture agree with the supplied InterPro/Pfam annotations. (liu2007functionalassociationof pages 1-2, li2015novelfunctionsof pages 6-10)
SUN1 is not an enzyme or transporter. Its primary function is as a membrane-embedded structural adaptor and force-transmission component of the LINC complex (“linker of nucleoskeleton and cytoskeleton”). Its nucleoplasmic N-terminal region engages lamins and other nuclear structures; its transmembrane/luminal region traverses the nuclear-envelope lumen; and its C-terminal SUN domain binds KASH-domain proteins in the outer nuclear membrane. KASH proteins then engage actin, intermediate filaments, microtubule motors, or specialized meiotic machinery. SUN1 thereby couples the nuclear lamina and chromosomes to cytoskeletal forces, controlling nuclear positioning, nuclear shape, cell migration, mechanotransduction, and meiotic chromosome movement. (gurusaran2023molecularinsightsinto pages 1-2, bougaran2024lifeatthe pages 3-5)
SUN1 also has LINC-adjacent functions at nuclear pore complexes (NPCs), including NPC distribution and NXF1-dependent mRNA export. Disease evidence indicates that too much or mislocalized SUN1 can be pathogenic in laminopathies, whereas loss or redistribution of SUN1 accompanies ALS/FTD nuclear pathology. These observations make SUN1 a potential therapeutic modifier, but there is presently no approved SUN1-directed treatment and no demonstrated human clinical efficacy. (li2017thefunctionof pages 1-2, chen2012accumulationofthe pages 9-11, sirtori2024linccomplexalterations pages 1-2)
The literature consistently distinguishes SUN1/UNC84A from the paralog SUN2/UNC84B. SUN1 and SUN2 are broadly expressed in mammalian somatic cells, whereas SUN3–SUN5 are primarily germline proteins. Human SUN1 and SUN2 reportedly have 46% overall sequence similarity, but their KASH-binding SUN domains are much more similar (82%) than their lamin-binding regions (19.7%), helping explain shared KASH binding but distinct nucleoplasmic interactions. (bougaran2024lifeatthe pages 3-5, kim2015makingthelinc pages 6-8)
No evidence encountered indicates that the queried symbol refers to another human protein. Results on plant SUN1 or C. elegans SUN-1/UNC-84 were excluded except where reviews used them for evolutionary context.
SUN1 is a type-II integral INM protein. Its N-terminal region projects into the nucleoplasm; a membrane-spanning region anchors it in the INM; and the C-terminal luminal region extends through the approximately 30–50-nm perinuclear space, ending in a conserved SUN domain near the outer nuclear membrane. Immunofluorescence, immunoelectron microscopy, and topology experiments directly support INM localization. At least two nucleoplasmic regions contribute to INM retention, whereas coordinated nucleoplasmic and luminal regions are needed for NPC association. (liu2007functionalassociationof pages 1-2)
The supplied domains—SUN1_N, Sun_CC2/coiled-coil elements, SUN domain, and HTH_SUN2-related family annotation—fit the experimentally supported architecture. The N-terminal region provides nuclear-side interactions; luminal coiled coils support oligomerization and span the nuclear lumen; and the C-terminal SUN domain forms the KASH-binding interface. The 2023 structure of a human SUN1 luminal coiled coil showed a trimeric assembly and, together with scattering, molecular dynamics, and modeling, suggested flexible connections between structured luminal domains and possible domain swapping in higher-order force-transmission networks. This full-length network remains a structural model rather than an intact-cell structure. (gurusaran2023molecularinsightsinto pages 1-2)
The most precise functional description is: SUN1 is the inner-nuclear-membrane anchor of nuclear-envelope-spanning LINC complexes. On the nuclear side, its N-terminus interacts with lamin A/C, more weakly with B-type lamins, emerin, and other nuclear-envelope or chromatin-associated proteins. On the luminal side, SUN1 oligomerizes and binds the short C-terminal KASH sequences of nesprins, KASH5, and LRMP/JAW1. The cytoplasmic regions of those KASH proteins connect to actin, intermediate filaments, kinesin, or dynein/dynactin. (kim2015makingthelinc pages 1-3, bougaran2024lifeatthe pages 3-5, gurusaran2023molecularinsightsinto pages 1-2)
Consequently, SUN1 does not catalyze a biochemical reaction and has no transported substrate. Its “substrate,” in a mechanical sense, is force: LINC complexes transmit tensile and reactive forces across the double nuclear membrane. Established outputs include nuclear anchorage and movement, nuclear morphology, cell polarity and migration, chromosome movement, and bidirectional mechanical communication between the nucleus and adhesion/cytoskeletal systems. (ueda2022innernuclearmembrane pages 1-2, gurusaran2023molecularinsightsinto pages 1-2)
The direct route from SUN1 to mammalian chromatin is incompletely resolved. Human-cell experiments support interactions with lamin-associated machinery, histone H2B, and DNA-dependent protein-kinase components, but a 2024 expert review emphasizes that direct SUN1–DNA binding has not been established in mammals. Therefore, “cytoskeleton-to-chromatin linkage” should usually be understood as lamina- and adaptor-mediated rather than proven direct DNA binding. (bougaran2024lifeatthe pages 3-5)
SUN1 can bind all six recognized mammalian KASH proteins, although partner expression and cytoskeletal adaptors confer biological specificity. Somatic nesprin-1/2 complexes connect principally to actin and motors; nesprin-3 connects through plectin to intermediate filaments; nesprin-4 engages kinesin; KASH5 is a meiosis-specific dynein-activating adaptor; and LRMP/JAW1 (KASH6) associates with microtubule-related organization. SUN1–nesprin-2 complexes have been associated preferentially with microtubule-dependent forward nuclear movement, whereas SUN2–nesprin-2 assemblies more strongly support actin-dependent rearward movement. The mechanism by which highly similar SUN domains discriminate among mechanically distinct complexes remains unresolved. (bougaran2024lifeatthe pages 3-5, gurusaran2023molecularinsightsinto pages 1-2)
| Function/domain | Molecular mechanism and location | Strongest evidence/model | Confidence/limitations |
|---|---|---|---|
| LINC force bridge | Type-II inner-nuclear-membrane protein whose nucleoplasmic N-terminus associates with lamins and other nuclear-envelope components. Luminal coiled coils and the C-terminal SUN domain bind outer-nuclear-membrane KASH proteins, coupling the nucleoskeleton to cytoskeletal filaments and motors. | Human-cell localization and interaction studies, mammalian genetics, and SUN–KASH structural and biophysical analyses. | High confidence for the bridge architecture and force-transmission role; partner selection, higher-order assembly, and direct coupling to mammalian chromatin remain incompletely resolved. |
| Nuclear pores and mRNA export | SUN1 concentrates near nuclear pore complexes, contributes to pore distribution, binds Nup153 and NXF1, and may transfer NXF1-containing messenger ribonucleoproteins to pores. PKC-regulated phosphorylation at SUN1 Ser113 modulates this pathway. | Immunofluorescence, immunoelectron microscopy, RNA interference, interaction assays, and poly(A)+ RNA-export rescue experiments in HeLa cells and human fibroblasts. | Moderate-to-high confidence in cultured cells; universal necessity in primary tissues or in vivo is unproven, and some effects may arise indirectly from altered nuclear-envelope organization. |
| Focal-adhesion reverse mechanotransduction | A SUN1-containing LINC connection supports actin organization and traction, enabling integrin-β1 activation and tension-dependent recruitment of vinculin, phosphorylated paxillin, and zyxin to maturing focal adhesions. | SUN1 knockdown and rescue, focal-adhesion imaging, adhesion assays, and traction-force measurements in cultured human epithelial and cancer-derived cells. | Moderate confidence; causal cell-culture evidence is strong, but tissue specificity and the immediate downstream effectors remain uncertain. |
| Meiosis and telomere movement | At the meiotic inner nuclear membrane, SUN1 connects telomere-associated TERB–MAJIN machinery to KASH5. KASH5 recruits dynein–dynactin, allowing microtubule forces to move chromosome ends and promote pairing, synapsis, and recombination. | Mammalian germ-cell localization and knockout studies, biochemical and structural work, and reported human genetic association with non-obstructive azoospermia. | High confidence in mice and for the conserved mammalian mechanism; human causal evidence is limited and individual variants require segregation and functional validation. |
| Laminopathies and LMNA cardiomyopathy | Abnormal lamin A or progerin states can produce SUN1 overaccumulation or mislocalization. Lowering SUN1 improves nuclear defects and senescence in patient fibroblasts and disrupts a harmful lamina–LINC connection in mouse laminopathy models. | Human HGPS fibroblast knockdown, Lmna-mutant and Sun1-deficient mice, and a 2023 in-vivo screen in cardiac-specific Lmna-deficient mice. | Strong preclinical evidence; SUN1 appears to be a downstream modifier rather than the initiating lesion. No validated SUN1-directed human therapy exists, and chronic inhibition could impair normal mechanics or fertility. |
| ALS/FTD | Loss or redistribution of SUN1, SUN2, and nesprins disrupts nuclear–cytoskeletal coupling and correlates with abnormal nuclear morphology, potentially contributing to pore injury, envelope rupture, and impaired nuclear homeostasis. | 2024 studies of C9ORF72-mutant human iPSC-derived neurons, spinal-cord organoids, and sporadic or C9-ALS postmortem central nervous system tissue. | Moderate disease-association evidence; complementary human models support relevance, but samples were limited and correlation does not establish SUN1 disruption as an initiating cause. |
| 2023 luminal SUN1 architecture | Crystallography, scattering, molecular dynamics, and modeling support a trimeric luminal coiled-coil assembly with flexible interdomain connections and possible domain swapping, offering a structural route for coordinated force transmission. | Purified human SUN1 fragments examined by X-ray crystallography and solution biophysics and integrated into a full-luminal-region model. | High confidence for the crystallized domain; the full-length configuration and proposed domain-swapped network await validation in intact nuclear membranes. |
| 2024 SUN1–KASH6 structural advance | The SUN1–JAW1/LRMP complex forms an asymmetric 9:6 assembly in which six KASH chains emerge from one molecular surface, providing geometry compatible with insertion of adjacent helices into the outer nuclear membrane. | X-ray crystal structure of the purified human SUN1–KASH6 complex. | High confidence for the crystallized complex; its prevalence in cells and applicability to canonical nesprin or KASH5 complexes remain unresolved. |
Table: A concise comparison of SUN1’s established molecular functions, disease associations, and recent structural advances, with the strongest supporting models and key interpretive limitations.
SUN1 participates in both conventional outside-to-nucleus mechanotransduction and reverse mechanotransduction from the nucleus toward the cytoskeleton and focal adhesions. In cultured human cells, SUN1 depletion left initial cell attachment and delivery of integrin-β1 to the plasma membrane largely intact but reduced active integrin-β1, disrupted actin organization and traction-force generation, and impaired tension-dependent incorporation of vinculin, phospho-paxillin, and zyxin into mature focal adhesions. Rescue with siRNA-resistant SUN1 restored key phenotypes. Total integrin-β1 rose by more than 1.5-fold after SUN1 depletion, while the active pool declined, arguing that the defect concerns force-dependent activation rather than integrin availability. (ueda2022innernuclearmembrane pages 1-2, ueda2022innernuclearmembrane pages 6-8)
This supports the pathway:
SUN1–KASH coupling → perinuclear/cellular actin organization → intracellular traction → integrin activation and focal-adhesion maturation → directional migration.
A 2024 study extended the general LINC-mechanotransduction framework to periodontal-ligament stem cells. Tension stress of 12% elongation at 0.5 Hz for 6 hours increased F-actin organization, nuclear area/pore size, YAP nuclear entry, and proliferation-related transcription; 24-hour stimulation produced the opposite proliferative outcome. Dominant-negative KASH disruption inhibited YAP translocation and proliferation, and a rat orthodontic model showed YAP nuclear localization and PCNA-positive cells peaking at day 7 and returning toward baseline by day 14. Because this experiment disrupted LINC complexes generally rather than SUN1 alone, it supports a SUN1-compatible mechanism but does not establish SUN1-specific necessity. (meng2024thecytoskeletondynamicsdependent pages 1-2, meng2024thecytoskeletondynamicsdependent pages 14-16)
SUN1, unlike SUN2, is concentrated near NPCs. RNAi depletion or dominant-negative SUN1 fragments caused NPC clustering, indicating that SUN1 helps distribute pores across the nuclear surface. This function requires coordinated nucleoplasmic and luminal regions rather than simply the conserved SUN domain. (liu2007functionalassociationof pages 1-2)
Human HeLa-cell and fibroblast studies further support a role in bulk, NXF1-dependent mRNA export. SUN1 directly associates with NXF1-containing messenger ribonucleoprotein complexes and with the nuclear-basket nucleoporin Nup153. The proposed handoff mechanism is:
mRNP–NXF1 capture by SUN1 at the nuclear envelope → transfer to Nup153/NPC → cytoplasmic export.
SUN1 depletion caused nuclear poly(A)+ RNA accumulation and was rescued by SUN1 re-expression. The experiments quantified nuclear/cytoplasmic RNA ratios in 500 cells per condition after 72-hour RNAi. PKC-dependent phosphorylation of SUN1 Ser113 reduced NXF1 interaction; nevertheless, the nonphosphorylatable S113A mutant rescued export less effectively than wild type, whereas phosphomimetic S113D supported efficient export, suggesting that regulated interaction cycling—not simply maximum binding—is functionally important. (li2017thefunctionof pages 1-2, li2015novelfunctionsof pages 79-82, li2015innernuclearenvelope pages 1-2)
This is a well-supported cultured-cell function, but its in-vivo tissue importance is less certain than SUN1’s structural LINC role.
During mammalian meiotic prophase I, telomeres attach to the nuclear envelope through a telomere complex containing TERB proteins and MAJIN, which interfaces with SUN1. Across the perinuclear space, SUN1 binds KASH5; KASH5 activates dynein/dynactin, coupling telomeres to microtubule forces. Rapid telomere-led chromosome movements facilitate homolog searching, pairing, synapsis, recombination, and crossing over. (kim2015makingthelinc pages 6-8, pawar2021thediversecellular pages 13-14, gurusaran2023molecularinsightsinto pages 1-2)
Mouse Sun1 loss impairs telomere attachment and KASH5 localization and causes meiotic failure/infertility; partial SUN2 compensation may explain residual attachment in some contexts. These animal data strongly establish the conserved mammalian mechanism. A 2023 Human Genetics report linked loss of SUN1 function in spermatocytes to defective telomere–nuclear-envelope attachment and non-obstructive azoospermia in humans (DOI: https://doi.org/10.1007/s00439-022-02515-z). However, full-text quantitative and segregation details were unavailable in the retrieved evidence, so this human association should be regarded as important but less independently assessable here than the mouse mechanism. (pereira2019nuclearenvelopedynamics pages 13-14)
SUN1 and SUN2 also facilitate membrane removal from chromatin during nuclear-envelope breakdown. Simultaneous depletion of human SUN proteins delays membrane clearance, consistent with a role in coordinating nuclear membranes with cytoskeletal/motor machinery during mitosis. This is an additional remodeling function rather than SUN1’s primary annotation, and redundancy with SUN2 limits SUN1-specific interpretation. (kim2015makingthelinc pages 14-15)
Gurusaran et al., 21 June 2023 resolved a trimeric SUN1 luminal coiled-coil domain and integrated crystallography, solution scattering, molecular dynamics, and modeling into a flexible luminal-region model. The work provides an architectural explanation for how SUN1 can span the nuclear lumen and coordinate force transmission. DOI: https://doi.org/10.3389/fcell.2023.1144277. (gurusaran2023molecularinsightsinto pages 1-2)
Gurusaran et al., January 2024 reported a crystal structure of SUN1 bound to LRMP/JAW1/KASH6 in an asymmetric 9:6 SUN1:KASH6 assembly. All six KASH chains emerge from one molecular surface, a geometry compatible with insertion of their adjacent transmembrane helices into the outer nuclear membrane. This helps resolve a steric problem posed by earlier symmetric SUN–KASH structures. Whether this architecture is common to nesprin- or KASH5-containing complexes in intact cells remains open. DOI: https://doi.org/10.1038/s42003-024-05794-6. (gurusaran2023molecularinsightsinto pages 1-2)
A 2024 study examined C9ORF72-mutant human iPSC-derived motor and cortical neurons, spinal-cord organoids, and postmortem spinal cord and motor cortex from sporadic and C9-associated ALS. Nuclear levels/distribution of SUN1, SUN2, nesprin-1, and nesprin-2 were severely altered. Abnormal SUN1 staining correlated with reduced nuclear area and circularity independently of TDP-43 mislocalization; one analysis included groups of 22, 21, 31, and 22 neurons, with several comparisons reaching p<0.0001. C9ORF72 repeat expansions account for approximately 40% of familial and 7% of sporadic ALS cases, situating the model in an important disease subset. DOI: https://doi.org/10.1186/s40478-024-01778-z; published April 2024. (sirtori2024linccomplexalterations pages 1-2, sirtori2024linccomplexalterations pages 10-12)
The study supports LINC disruption as a candidate early biomarker or pathogenic contributor, but not yet as a proven initiating cause. Postmortem specimens represent late disease, iPSC neurons are developmentally immature, and cohort sizes were limited. Accordingly, therapeutic targeting is exploratory. (sirtori2024linccomplexalterations pages 10-12)
A 2023 in-vivo screen tested 14 candidate interventions in cardiac-specific Lmna-deficient mice. Sun1 shRNA improved cardiac function and, together with Lamin C supplementation, produced the most durable survival benefit, correlating with reduced inflammation and DNA damage. Across treatment groups, disease markers correlated negatively with ejection fraction (Spearman −0.640 to −0.921) and survival (−0.782 to −0.927). The authors also reported that dominant-negative SUN1 delivered after ejection fraction had begun to decline prolonged survival in an inducible model, indicating treatment rather than purely prophylactic potential. DOI: https://doi.org/10.1186/s12967-023-04542-4; published October 2023. (tan2023systematicinvivo pages 14-16, tan2023systematicinvivo pages 1-3)
This remains mouse/AAV evidence. Broad or chronic SUN1 suppression could compromise normal mechanotransduction, nuclear positioning, NPC organization, and fertility; tissue-restricted dosing and long-term safety therefore require study.
SUN1 appears to be a disease modifier and downstream effector of abnormal lamin-A states. In Lmna-null and progeroid LmnaΔ9 mice, concomitant Sun1 deficiency reduced tissue pathology and extended survival; all LmnaΔ9 animals died by 30 days, whereas most LmnaΔ9/Sun1-deficient littermates lived more than twice as long. In HGPS fibroblasts, SUN1 knockdown improved nuclear morphology, heterochromatin markers, and cellular senescence. One heterochromatin analysis quantified 154 control-RNAi and 157 SUN1-RNAi cells, and the nuclear-morphology experiments scored 200 mock-transfected or 50 SUN1-transfected cells per sample. (chen2012accumulationofthe pages 9-11, chen2012accumulationofthe pages 1-2)
Mechanistically, overaccumulation arose from reduced SUN1 protein turnover rather than increased transcription. The authors proposed that excessive SUN1 stiffens or disorganizes nuclear-envelope networks downstream of progerin/abnormal lamin A. This is compelling modifier evidence, but it does not mean that SUN1 mutation causes classic HGPS; the initiating lesion is generally LMNA/progerin. DOI: https://doi.org/10.1016/j.cell.2012.01.059; published 27 April 2012. (chen2012accumulationofthe pages 9-11, chen2012accumulationofthe pages 1-2)
SUN1 variants reported in muscular-dystrophy patients can retain nuclear-envelope localization while showing reduced lamin-A/C recovery in biochemical assays. Because SUN1/SUN2 variants may coexist with mutations in established nuclear-envelope disease genes, pathogenicity should be assigned only with segregation, population, and functional evidence. (li2015novelfunctionsof pages 29-36)
The strongest biological case for a direct SUN1-loss phenotype is meiotic infertility: disruption of the SUN1–KASH5 telomere bridge prevents correct chromosome movement and prophase progression. Mouse evidence is extensive, and emerging human genetic data implicate SUN1 loss in non-obstructive azoospermia. At present, SUN1 testing may be relevant in research-grade infertility gene panels, but it is not by itself a validated standalone clinical diagnostic or therapeutic target. (pereira2019nuclearenvelopedynamics pages 13-14, gurusaran2023molecularinsightsinto pages 1-2)
The 2024 ALS/FTD findings make SUN1 localization and broader LINC integrity candidate tissue or imaging biomarkers. However, abnormal SUN1 in ALS may be causal, compensatory, or secondary to nuclear-envelope stress. The most defensible current application is mechanistic disease stratification in patient-derived neurons and organoids—not clinical diagnosis or treatment. (sirtori2024linccomplexalterations pages 1-2, sirtori2024linccomplexalterations pages 10-12)
LINC-dependent control of YAP nuclear entry in periodontal stem cells offers a mechanistic basis for optimizing mechanical loading in tissue engineering or orthodontic remodeling. Nevertheless, the intervention used dominant-negative KASH and cannot assign the effect solely to SUN1; translation to clinical loading protocols remains conceptual. (meng2024thecytoskeletondynamicsdependent pages 1-2, meng2024thecytoskeletondynamicsdependent pages 14-16)
Established core annotation—high confidence: SUN1 is a type-II INM structural adaptor that forms SUN–KASH LINC bridges and transmits forces between nucleoskeleton/chromosome-associated structures and the cytoskeleton. This conclusion is supported by topology, interaction, genetic, and structural studies. (kim2015makingthelinc pages 1-3, liu2007functionalassociationof pages 1-2, gurusaran2023molecularinsightsinto pages 1-2)
Primary location—high confidence: Its functional center is the inner nuclear membrane and perinuclear lumen, with a specialized pool associated with NPCs. SUN1 may transiently misaccumulate in Golgi/ER-related membranes in laminopathy models, but that is pathological rather than its normal principal location. (chen2012accumulationofthe pages 9-11, liu2007functionalassociationof pages 1-2)
Meiosis—high confidence in mammals, moderate in humans: The SUN1–KASH5 bridge transmits dynein/microtubule forces to telomeres. Human infertility genetics is emerging but less extensive than mouse evidence. (pereira2019nuclearenvelopedynamics pages 13-14, gurusaran2023molecularinsightsinto pages 1-2)
mRNA export and NPC distribution—moderate-to-high cell-biological confidence: Direct interactions and rescue studies are persuasive, although organism-level physiological importance and tissue specificity remain incompletely tested. (li2017thefunctionof pages 1-2, liu2007functionalassociationof pages 1-2)
Disease targeting—promising but preclinical: Reducing SUN1 can rescue laminopathy phenotypes in cells and mice, yet SUN1 also performs essential normal mechanical and reproductive functions. A therapeutic window, delivery strategy, and human efficacy have not been established. (chen2012accumulationofthe pages 9-11, tan2023systematicinvivo pages 14-16, tan2023systematicinvivo pages 1-3)
Human SUN1/O94901 is best annotated as an inner-nuclear-membrane mechanical adaptor and organizer. Its defining activity is assembly of LINC bridges: the N-terminal nuclear region anchors to lamina-associated structures, while luminal coiled coils and the C-terminal SUN domain oligomerize and bind KASH partners in the outer nuclear membrane. This architecture converts cytoskeletal motor and filament forces into nuclear positioning, shape control, mechanotransduction, and—through KASH5—meiotic telomere movement. A distinct NPC-associated pool contributes to pore distribution and NXF1-dependent mRNA export. Recent structural studies have refined the geometry and flexibility of SUN1 assemblies, while disease studies identify SUN1 as a potentially actionable modifier of laminopathy/cardiomyopathy and as a marker or contributor to ALS/FTD nuclear pathology. The translational evidence is promising but remains preclinical; SUN1’s essential physiological functions make selective, tissue-specific modulation more plausible than systemic inhibition.
References
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