Affinage

TMEM43

Transmembrane protein 43 · UniProt Q9BTV4

Length
400 aa
Mass
44.9 kDa
Annotated
2026-06-10
52 papers in source corpus 22 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TMEM43 (LUMA) is a four-transmembrane-domain integral membrane protein that functions as a structural scaffold at the inner nuclear membrane and the ER/SR membrane, where it organizes nuclear envelope architecture and membrane contact sites (PMID:18230648, PMID:41919408). At the nuclear envelope it homooligomerizes through its membrane spans, binds A- and B-type lamins (including lamin B2) and depends on A-type lamins for its localization, and tethers emerin and SUN2; loss of TMEM43 or expression of oligomerization-defective mutants redistributes emerin and SUN2 and produces abnormally shaped nuclei (PMID:18230648, PMID:21391237, PMID:40948388). Beyond the nuclear envelope, TMEM43 localizes to the ER/SR membrane and to cytoplasmic plaques of adhering and composite junctions, including cardiac intercalated disks (PMID:24770932, PMID:41919408), and it bridges the ER/SR to mitochondria by binding the outer-mitochondrial-membrane channels VDAC1/VDAC2 (Porin) to stabilize ER-mitochondrial contact sites (PMID:41236655, PMID:41411330). The dominant arrhythmogenic cardiomyopathy mutation p.S358L destabilizes the protein and abolishes VDAC binding, collapsing mitochondrial membrane potential, raising ROS, and impairing lipid metabolism and ATP production (PMID:41236655, PMID:41411330, PMID:41919408); in parallel it mislocalizes lamin B2, closes chromatin at the RYR2 promoter, and downregulates RYR2 to drive SR Ca²⁺ leak and arrhythmia (PMID:40948388). Loss of TMEM43 in cardiac myocytes activates a DNA-damage-response–TP53–SASP cascade and NF-κB–TGFβ signaling that produces pro-fibrotic cardiomyopathy (PMID:29980933, PMID:33070193), and restoring wild-type TMEM43 by transgene or AAV9 delivery suppresses the S358L disease phenotype (PMID:40091736). In non-cardiac contexts TMEM43 acts as a signaling scaffold, mediating EGFR-induced NF-κB activation via CARMA3 (PMID:27991920) and maintaining passive conductance in cochlear glia-like supporting cells through interaction with connexins and the KCNK3 (TASK-1) channel, with a nonsense variant causing auditory neuropathy (PMID:34050020, PMID:34737237).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2008 High

    Established TMEM43's basic identity and topology — whether it was a bona fide nuclear envelope protein and how it integrated into the lamina — by defining its membrane topology and its physical partners.

    Evidence Protease protection, epitope accessibility, co-IP and dominant-negative imaging in mammalian cells

    PMID:18230648

    Open questions at the time
    • Functional consequence of lamin/emerin binding for nuclear mechanics not measured
    • Non-nuclear localization not addressed
  2. 2011 High

    Extended the scaffold model to the LINC complex by showing TMEM43 binds SUN2 and that a disease mutation disrupts oligomerization and mislocalizes partners, linking TMEM43 dysfunction to nuclear shape defects.

    Evidence Co-IP, immunofluorescence and in vivo muscle electroporation of mutant LUMA

    PMID:21391237

    Open questions at the time
    • Mechanical/physiological readout of partner mislocalization not quantified
    • Tissue specificity of phenotype unresolved
  3. 2014 Medium

    Connected genotype to a biophysical phenotype and revealed non-nuclear localization, showing the p.S358L mutation stiffens nuclei and that TMEM43 resides in junctional plaques as well as the nuclear envelope.

    Evidence Atomic force microscopy on patient fibroblasts; immunolocalization across tissues

    PMID:24598986 PMID:24770932

    Open questions at the time
    • Single-lab AFM measurement
    • Junction localization lacks functional perturbation
  4. 2016 High

    Identified an unexpected signaling role: that TMEM43 is a required scaffold in EGFR-induced NF-κB activation, broadening its function beyond a structural envelope protein.

    Evidence BiFC functional genomics screen, co-IP, knockdown and in vivo tumor models

    PMID:27991920

    Open questions at the time
    • Relationship between signaling role and nuclear/junctional functions unclear
    • Direct EGFR-TMEM43 contact not structurally defined
  5. 2018 High

    Tested whether TMEM43 is required for the heart and whether S358L is intrinsically pathogenic, yielding conflicting models: a knock-in drove NF-κB–TGFβ fibrosis while an independent null/knock-in showed normal cardiac function.

    Evidence S358L knock-in and germline-null mouse models, NF-κB reporters, echocardiography, pressure overload

    PMID:29040414 PMID:29980933

    Open questions at the time
    • Discordant cardiac phenotypes between models unresolved
    • Genetic background and dosage effects not reconciled
  6. 2021 High

    Defined a cardiac fibrosis mechanism via loss of function, showing myocyte TMEM43 haploinsufficiency activates a DDR→TP53→SASP axis driving SMAD2/3 and age-dependent cardiomyopathy.

    Evidence Cardiac-specific conditional knockout mouse, transcriptomics, immunoblotting, histology

    PMID:33070193

    Open questions at the time
    • Whether loss-of-function recapitulates the dominant S358L disease mechanism unclear
    • Trigger linking TMEM43 loss to DNA damage undefined
  7. 2021 High

    Established a distinct sensory function and a second disease, showing TMEM43 binds connexins and the KCNK3/TASK-1 channel to set passive conductance in cochlear supporting cells, with a nonsense variant causing auditory neuropathy.

    Evidence Linkage/exome sequencing, knock-in mouse, electrophysiology, co-IP/PLA and domain-deletion mapping

    PMID:34050020 PMID:34737237

    Open questions at the time
    • Whether TMEM43 itself conducts ions or only scaffolds channels unresolved
    • Intracellular loop interaction not structurally defined
  8. 2022 Medium

    Implicated TMEM43 in metabolism, redox balance and cancer, connecting it to ferroptosis suppression, mTOR-driven hypertrophy, lipid/energy homeostasis, and tumor-promoting partners PRPF3 and RAP2B/ERK.

    Evidence AAV9 cardiac models, zebrafish transgenics/CRISPR, Drosophila ortholog models, co-IP/MS and metabolomics

    PMID:35260078 PMID:35869176 PMID:36076925 PMID:36230956

    Open questions at the time
    • Mechanistic link between membrane scaffolding and ferroptosis/mTOR not established
    • Cancer partner interactions are single-lab co-IP findings
  9. 2023 Medium

    Connected the mutation to developmental signaling, showing S358L diminishes cardiac β-catenin while driving nuclear plakoglobin translocation, with organ-specific WNT pathway alterations.

    Evidence S358L knock-in mouse, immunohistochemistry, microarray, electron microscopy

    PMID:37083466

    Open questions at the time
    • Causal direction between TMEM43 loss and WNT dysregulation unclear
    • Single-lab model
  10. 2025 High

    Converged the field on ER-mitochondrial contact sites as the core pathomechanism, showing TMEM43 binds VDAC1/2 to stabilize these junctions and that S358L abolishes binding, collapsing mitochondrial function, energy and lipid homeostasis across fly, hiPSC-CM and human myocardium.

    Evidence IP-MS, TurboID proximity labeling, Drosophila interaction assays, lipidomics/proteomics/metabolomics, mitochondrial assays in patient-derived cells and tissue

    PMID:41236655 PMID:41411330 PMID:41919408

    Open questions at the time
    • Structural basis of the TMEM43-VDAC interface not resolved
    • Quantitative contribution of contact-site loss versus other mechanisms not partitioned
  11. 2025 High

    Linked the nuclear scaffolding role directly to arrhythmia, showing mutant TMEM43 mislocalizes lamin B2, closes RYR2 promoter chromatin, downregulates RYR2 and produces SR Ca²⁺ leak preventable by flecainide.

    Evidence Patient iPSC-CMs, co-IP, super-resolution imaging, chromatin accessibility assay, Ca²⁺ imaging, knock-in mouse, drug treatment

    PMID:40948388

    Open questions at the time
    • How a single mutation simultaneously disrupts nuclear and ER-mitochondrial functions unresolved
    • Generalizability beyond P386S/S358L variants
  12. 2025 High

    Provided proof-of-concept therapy, showing wild-type TMEM43 transgene or AAV9 delivery suppresses the dominant S358L disease, indicating restoration of normal TMEM43 dosage is protective.

    Evidence Double transgenic mice, AAV9 gene delivery, echocardiography, ECG, histology, survival

    PMID:40091736

    Open questions at the time
    • Molecular basis of dominance/rescue not mechanistically dissected
    • Durability and translational dosing not addressed

Open questions

Synthesis pass · forward-looking unresolved questions
  • How a single membrane scaffold coordinates nuclear envelope mechanics, junctional integrity, ER-mitochondrial contact, and channel/signaling functions — and which of these is primary in each disease — remains unresolved.
  • No structure of TMEM43 or its complexes
  • Conflicting cardiac models (fibrosis vs. dispensable) not reconciled
  • Unified mechanism linking nuclear, mitochondrial and signaling roles absent

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 5 GO:0005198 structural molecule activity 2
Localization
GO:0005635 nuclear envelope 4 GO:0005783 endoplasmic reticulum 2 GO:0005886 plasma membrane 1
Pathway
R-HSA-1430728 Metabolism 3 R-HSA-162582 Signal Transduction 2
Partners
CARMA3EMDKCNK3LMNALMNB2SUN2VDAC1VDAC2
Complex memberships
LINC complex

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2008 LUMA (TMEM43) is an integral inner nuclear membrane (INM) protein with four transmembrane domains and a large hydrophilic domain located between membrane spans 1 and 2 exposed to the perinuclear space, with both termini residing cyto- or nucleoplasmically. Nuclear envelope targeting mainly depends on the membrane spans. Transmembrane domains also promote homooligomerization. LUMA binds A- and B-type lamins and depends on A-type lamins for its INM localization. LUMA interacts with emerin, and both downregulation of LUMA and overexpression of dominant-negative LUMA fragments causes redistribution of emerin. Protease protection assay, antibody epitope accessibility assay, co-immunoprecipitation, dominant-negative overexpression, immunofluorescence Journal of cell science High 18230648
2011 TMEM43 (LUMA) interacts with SUN2 (in addition to emerin) at the nuclear membrane. The p.Glu85Lys mutation in TMEM43 causes failure of oligomerization, reduced nuclear staining of LUMA, and redistribution/aggregation of emerin and SUN2, along with a higher proportion of abnormally shaped nuclei. In vivo electroporation of mutant LUMA in mouse tibialis anterior muscles similarly showed decreased staining of emerin and SUN2 on myonuclei. In vitro transfection, co-immunoprecipitation, immunofluorescence, in vivo electroporation in mouse muscle Annals of neurology High 21391237
2014 Skin fibroblasts from carriers of the TMEM43 p.S358L mutation exhibit increased nuclear stiffness compared to wild-type controls, as measured by atomic force microscopy, suggesting that the mutation affects nuclear mechanical properties. Atomic force microscopy on patient-derived skin fibroblasts European heart journal Medium 24598986
2014 In mammalian cells, LUMA (TMEM43) localizes not only at the nuclear envelope but also as a cytoplasmic plaque constituent of zonula adhaerens and punctum adhaerens in diverse epithelia and in composite junctions (CJs) of myocardiac intercalated disks, where it colocalizes with other CJ marker proteins. Immunolocalization with high-specificity antibodies in diverse mammalian tissues and cell cultures Cell and tissue research Medium 24770932
2016 TMEM43/LUMA is a critical component of the EGFR signaling network that mediates EGFR-induced NF-κB activation. Upon EGF stimulation, EGFR recruits TMEM43, which then interacts with the scaffold protein CARMA3 and its associating complex to induce downstream NF-κB activation. TMEM43 deficiency impairs colony formation, anoikis resistance, migration, invasion, and tumor progression in vivo. Bimolecular Fluorescence Complementation-based functional genomics screen, co-immunoprecipitation, knockdown studies, in vitro functional assays, in vivo tumor models Oncogene High 27991920
2018 The TMEM43 S358L mutation leads to hyper-activated NF-κB signaling in heart tissues and primary cardiomyocytes, which directly drives expression of pro-fibrotic TGFβ1 and enhances downstream TGFβ signaling, contributing to cardiac fibrosis in ARVC. TMEM43 S358L knock-in mouse model, NF-κB reporter assays, gene expression analysis in heart tissue and primary cardiomyocytes Protein & cell Medium 29980933
2018 TMEM43 (Luma) is dispensable for murine cardiac development and function; germline null mice are viable with normal cardiac function and normal response to pressure overload. Localization and expression of other LINC complex components in cardiac myocytes and fibroblasts is unaffected by global loss of Luma. Furthermore, Luma S358L knock-in mice display normal cardiac function and morphology. Germline null mouse generation, Luma S358L knock-in mouse generation, echocardiography, transverse aortic constriction, immunofluorescence, immunoblotting Cardiovascular research High 29040414
2021 Haploinsufficiency of Tmem43 in cardiac myocytes (Myh6-Cre:Tmem43W/F mice) activates the DNA damage response (DDR) and TP53 pathway, leading to increased senescence-associated secretory phenotype (SASP) markers and downstream phospho-SMAD2/phospho-SMAD3 activation, resulting in age-dependent pro-fibrotic cardiomyopathy with fibrosis, adipogenesis, and apoptosis. Cardiac-specific conditional knockout mouse model (Myh6-Cre x floxed Tmem43), cardiac myocyte transcriptome sequencing, immunoblotting for DDR/TP53/SASP markers, histology Cardiovascular research High 33070193
2021 A nonsense variant in TMEM43 (p.Arg372Ter) causes auditory neuropathy spectrum disorder (ANSD). TMEM43 physically interacts with Connexin26 and Connexin30 gap junction channels in cochlear glia-like supporting cells (GLSs). The p.Arg372Ter variant disrupts passive conductance current in GLSs in a dominant-negative fashion. Linkage analysis and exome sequencing, knock-in mouse model, electrophysiology (passive conductance current measurement), co-immunoprecipitation/interaction assays Proceedings of the National Academy of Sciences of the United States of America High 34050020
2021 TMEM43 physically interacts with the KCNK3 (TASK-1) two-pore domain K+ channel in the cochlea. The intracellular loop domain of TMEM43 is responsible for TASK-1 binding. Gene silencing of Task-1 results in significantly reduced passive conductance current in cochlear glia-like supporting cells. Co-immunoprecipitation, Duolink proximity ligation assay, domain deletion analysis, siRNA knockdown with electrophysiology Experimental neurobiology High 34737237
2022 TMEM43 overexpression inhibits LPS-induced ferroptosis in cardiomyocytes by suppressing P53 and ferritin levels while enhancing GPX4 and SLC7A11 expression. TMEM43 knockdown aggravates LPS-induced lipid peroxidation and ferroptosis. AAV9-mediated cardiac overexpression/knockdown in mice, siRNA/adenoviral overexpression in H9c2 cells, ferroptosis markers (MDA, iron density, GPX4, SLC7A11), ferrostatin-1 rescue experiment Cells Medium 36230956
2022 In a zebrafish model, the p.S358L mutant TMEM43 protein is unstable and partially redistributes from the nuclear membrane into the cytoplasm in embryonic and adult hearts. Overexpression of wild-type TMEM43 activates the mTOR pathway and ribosome biogenesis, leading to cardiomyocyte hypertrophy. Transgenic zebrafish overexpression lines (Tol2-system), CRISPR/Cas9 knockout, immunofluorescence, transcriptomic profiling, electron microscopy International journal of molecular sciences Medium 36076925
2022 TMEM43 promotes pancreatic cancer progression by stabilizing PRPF3 (preventing its degradation) and by regulating the RAP2B/ERK signaling axis, as identified by co-immunoprecipitation followed by mass spectrometry. Co-immunoprecipitation, protein mass spectrometry, in vitro knockdown/overexpression assays, in vivo tumorigenicity assay Cellular & molecular biology letters Medium 35260078
2022 In the TMEM43 S358L Drosophila model, the conserved serine at position 333 (homologous to human S358) is critical for physiological function. The S333L substitution causes impaired energy homeostasis and lipid metabolism, cardiac arrhythmias, and premature death. Similar metabolic impairments were confirmed in a murine Tmem43 disease model. CRISPR/Cas9 CG8111 knockout, transgenic overexpression of CG8111 p.S333L in Drosophila, metabolomic and proteomic analyses, cardiac function assay in flies Cellular and molecular life sciences : CMLS Medium 35869176
2023 In the TMEM43 S358L knock-in mouse model, TMEM43 and β-catenin expression are diminished in the heart while junctional plakoglobin (JUP) translocates into nuclei of mutant cardiomyocytes, indicating dysregulation of the WNT-β-catenin pathway. Conversely, in the small intestine of mutants, β-catenin and Ki-67 are overexpressed alongside elongated villi and fatty infiltration, indicating organ-specific pathway alterations. Knock-in mouse model (heterozygous and homozygous), immunohistochemistry, microarray transcriptome analysis, protein expression analysis, electron microscopy, histology American journal of physiology. Heart and circulatory physiology Medium 37083466
2024 USP7 deubiquitinase regulates TMEM43 protein stability through deubiquitination. TMEM43 in turn interacts with and activates VDAC1, promoting hepatocellular carcinoma progression through a USP7/TMEM43/VDAC1 axis. Co-immunoprecipitation, western blot for ubiquitination, CCK-8, flow cytometry, Transwell assays Translational gastroenterology and hepatology Medium 38317750
2025 TMEM43 localizes at the ER/SR membrane and interacts with the outer mitochondrial membrane protein VDAC (Porin) in Drosophila. The p.S333L mutation (analogous to human p.S358L) abolishes this interaction, causing breakdown of mitochondrial membrane potential, increased reactive oxygen species, and severe mitochondrial ultrastructural defects. Similar mitochondrial ultrastructural defects were observed in human right ventricular myocardium from TMEM43 p.S358L carriers, suggesting impaired ER/SR-mitochondrial contact sites as a key pathomechanism. Immunofluorescence localization, protein interaction assays (Drosophila), mitochondrial membrane potential assay, ROS measurement, ultrastructural electron microscopy (Drosophila and human cardiac tissue) Cellular and molecular life sciences : CMLS High 41236655
2025 Proteomic screening by quantitative IP-mass spectrometry identified 166 differential binding partners of TMEM43 vs. TMEM43 p.S358L. VDAC1 and VDAC2 binding to the TMEM43 p.S358L mutant is significantly decreased. Reduced VDAC binding mediates mitochondrial dysfunction in H9c2 cardiac myoblasts expressing TMEM43 p.S358L. Quantitative immunoprecipitation-mass spectrometry, immunofluorescence, TurboID proximity labeling, mitochondrial functional assays in H9c2 cells PloS one Medium 41411330
2025 TMEM43 localizes in the endoplasmic reticulum and nuclear lamina. The p.S358L mutation alters interaction with proteins of ER and mitochondrial membranes. Mutant hiPSC-CMs show lipid accumulation, decreased lipid metabolism capacity, lower ATP:ADP ratio, and diminished contraction frequency. Pull-down experiments reveal differential interacting proteins at ER-mitochondrial contact sites, suggesting that the mutation impairs ER-mitochondrial interactions affecting lipid homeostasis and energy supply. Sucrose-gradient ultracentrifugation, mass spectrometry, HA-tag pull-down, lipidomics, proteomics, ATP/ADP measurement, contractility assay in hiPSC-CMs, metabolomics in human myocardium Circulation. Genomic and precision medicine High 41919408
2025 TMEM43 interacts with lamin B2. The TMEM43-P386S mutation induces lamin B2 mislocalization and abnormal nuclear envelope structure in ARVC iPSC-CMs, resulting in decreased chromatin accessibility at promoters of downregulated genes including RYR2. RYR2 proteins are downregulated and grouped into smaller clusters, contributing to enhanced SR Ca2+ leak and arrhythmic phenotype. This phenotype was preventable by flecainide. iPSC-CMs from mutation carriers, co-immunoprecipitation (TMEM43-lamin B2), Tau-STED super-resolution imaging (RYR2 clusters), chromatin accessibility assay, Ca2+ imaging, knock-in mouse model, flecainide treatment Advanced science High 40948388
2025 Overexpression of wild-type TMEM43 in double transgenic mice (expressing both WT and S358L TMEM43) delays ARVC5 onset, improves cardiac contraction, reduces cardiomyocyte death and myocardial fibrosis, and improves survival. Systemic delivery of AAV9 carrying codon-optimized WT-TMEM43 prevents ventricular dysfunction and ECG abnormalities induced by S358L-TMEM43 in mice. Double transgenic mouse model (WT + S358L TMEM43), AAV9 gene delivery, echocardiography, ECG, histology, survival analysis Circulation research High 40091736
2026 In a Drosophila CRISPR/Cas9 knock-in model of Tmem43 p.S333L (equivalent to human p.S358L), flies show reduced lifespan, smaller body size, lipid droplet accumulation, and mitochondrial defects. Proteomic and lipidomic profiling revealed misregulation of energy metabolism, reduced fatty acid synthesis and β-oxidation, altered peroxisomal pathways, elevated phosphatidylethanolamine and phosphatidylinositol levels, and reduced triacylglycerols. Ultrastructural analyses confirmed mitochondrial degradation in muscle tissue. CRISPR/Cas9 knock-in Drosophila model, lipidomics, proteomics, electron microscopy, fatty acid oxidation assays Biology open Medium 41873591

Source papers

Stage 0 corpus · 52 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2008 Arrhythmogenic right ventricular cardiomyopathy type 5 is a fully penetrant, lethal arrhythmic disorder caused by a missense mutation in the TMEM43 gene. American journal of human genetics 392 18313022
2006 LUMA (LUminometric Methylation Assay)--a high throughput method to the analysis of genomic DNA methylation. Experimental cell research 228 16624287
2006 Using LUMA: a Luminometric-based assay for global DNA-methylation. Epigenetics 141 17998810
2005 The impact of implantable cardioverter-defibrillator therapy on survival in autosomal-dominant arrhythmogenic right ventricular cardiomyopathy (ARVD5). Journal of the American College of Cardiology 127 15680719
2011 TMEM43 mutations in Emery-Dreifuss muscular dystrophy-related myopathy. Annals of neurology 93 21391237
2012 The natural history of a genetic subtype of arrhythmogenic right ventricular cardiomyopathy caused by a p.S358L mutation in TMEM43. Clinical genetics 82 22725725
2008 LUMA interacts with emerin and influences its distribution at the inner nuclear membrane. Journal of cell science 74 18230648
2012 DNA methylation in peripheral blood measured by LUMA is associated with breast cancer in a population-based study. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 70 22371529
2014 The TMEM43 Newfoundland mutation p.S358L causing ARVC-5 was imported from Europe and increases the stiffness of the cell nucleus. European heart journal 68 24598986
2011 Mutation analysis and evaluation of the cardiac localization of TMEM43 in arrhythmogenic right ventricular cardiomyopathy. Clinical genetics 65 21214875
2016 Long-Term Clinical Outcome of Arrhythmogenic Right Ventricular Cardiomyopathy in Individuals With a p.S358L Mutation in TMEM43 Following Implantable Cardioverter Defibrillator Therapy. Circulation. Arrhythmia and electrophysiology 57 26966288
2022 TMEM43 Protects against Sepsis-Induced Cardiac Injury via Inhibiting Ferroptosis in Mice. Cells 49 36230956
2021 Haploinsufficiency of Tmem43 in cardiac myocytes activates the DNA damage response pathway leading to a late-onset senescence-associated pro-fibrotic cardiomyopathy. Cardiovascular research 49 33070193
2014 Global methylation levels in peripheral blood leukocyte DNA by LUMA and breast cancer: a case-control study in Japanese women. British journal of cancer 47 24786600
2012 Recurrent missense mutations in TMEM43 (ARVD5) due to founder effects cause arrhythmogenic cardiomyopathies in the UK and Canada. European heart journal 45 23161701
2018 Luma is not essential for murine cardiac development and function. Cardiovascular research 40 29040414
2018 TMEM43-S358L mutation enhances NF-κB-TGFβ signal cascade in arrhythmogenic right ventricular dysplasia/cardiomyopathy. Protein & cell 39 29980933
2013 TMEM43 mutations associated with arrhythmogenic right ventricular cardiomyopathy in non-Newfoundland populations. Human genetics 39 23812740
2016 TMEM43/LUMA is a key signaling component mediating EGFR-induced NF-κB activation and tumor progression. Oncogene 37 27991920
2020 Clinical characteristics and determinants of the phenotype in TMEM43 arrhythmogenic right ventricular cardiomyopathy type 5. Heart rhythm 35 32062046
2020 Exercise and arrhythmic risk in TMEM43 p.S358L arrhythmogenic right ventricular cardiomyopathy. Heart rhythm 32 32120009
2021 A nonsense TMEM43 variant leads to disruption of connexin-linked function and autosomal dominant auditory neuropathy spectrum disorder. Proceedings of the National Academy of Sciences of the United States of America 28 34050020
2021 Systems genetics analysis defines importance of TMEM43/LUMA for cardiac- and metabolic-related pathways. Physiological genomics 28 34766515
2014 Protein LUMA is a cytoplasmic plaque constituent of various epithelial adherens junctions and composite junctions of myocardial intercalated disks: a unifying finding for cell biology and cardiology. Cell and tissue research 23 24770932
2013 DNA isolation method is a source of global DNA methylation variability measured with LUMA. Experimental analysis and a systematic review. PloS one 19 23585847
2022 TMEM43 promotes pancreatic cancer progression by stabilizing PRPF3 and regulating RAP2B/ERK axis. Cellular & molecular biology letters 17 35260078
2012 Functional effects of the TMEM43 Ser358Leu mutation in the pathogenesis of arrhythmogenic right ventricular cardiomyopathy. BMC medical genetics 17 22458570
2022 Altered Expression of TMEM43 Causes Abnormal Cardiac Structure and Function in Zebrafish. International journal of molecular sciences 14 36076925
2007 LUMA cervical imaging system. Expert review of medical devices 12 17359219
2020 Canine prostatic cancer cell line (LuMa) with osteoblastic bone metastasis. The Prostate 11 32348616
2020 Human pluripotent stem cell line (HDZi001-A) derived from a patient carrying the ARVC-5 associated mutation TMEM43-p.S358L. Stem cell research 11 32858485
2022 A Drosophila melanogaster model for TMEM43-related arrhythmogenic right ventricular cardiomyopathy type 5. Cellular and molecular life sciences : CMLS 10 35869176
2022 Adipogenic Signaling Promotes Arrhythmia Substrates before Structural Abnormalities in TMEM43 ARVC. Journal of personalized medicine 10 36294819
2016 Fetal arrhythmogenic right ventricular cardiomyopathy with double mutations in TMEM43. Pediatrics international : official journal of the Japan Pediatric Society 10 26840987
2023 The TMEM43 S358L mutation affects cardiac, small intestine, and metabolic homeostasis in a knock-in mouse model. American journal of physiology. Heart and circulatory physiology 9 37083466
2022 Urinary parabens and breast cancer risk: Modification by LINE-1 and LUMA global DNA methylation, and associations with breast cancer defined by tumor promoter methylation status. Molecular carcinogenesis 7 35975911
2021 A Deafness Associated Protein TMEM43 Interacts with KCNK3 (TASK-1) Two-pore Domain K+ (K2P) Channel in the Cochlea. Experimental neurobiology 7 34737237
2015 Global Analysis of DNA 5-Methylcytosine Using the Luminometric Methylation Assay, LUMA. Methods in molecular biology (Clifton, N.J.) 7 26103902
2025 Overexpression of Wild-Type TMEM43 Improves Cardiac Function in Arrhythmogenic Right Ventricular Cardiomyopathy Type 5. Circulation research 6 40091736
2024 TMEM43 promotes the development of hepatocellular carcinoma by activating VDAC1 through USP7 deubiquitination. Translational gastroenterology and hepatology 6 38317750
2017 Ventricular tachycardia ablation in arrhythmogenic right ventricular cardiomyopathy patients with TMEM43 gene mutations. Journal of cardiovascular electrophysiology 6 28960618
2015 Global DNA Methylation, Measured by the Luminometric Methylation Assay (LUMA), Associates with Postmenopausal Breast Cancer in Non-Obese and Physically Active Women. Journal of Cancer 6 26000047
2024 Generation of a TMEM43 knockout human induced pluripotent stem cell line (HDZi003-A-1) using CRISPR/Cas9. Stem cell research 4 38430734
2025 The ARVC-5-associated protein TMEM43 controls mitochondrial energy metabolism by stabilising ER-mitochondrial contact sites. Cellular and molecular life sciences : CMLS 3 41236655
2024 Real-Life Data of 2-Year Lumasiran Use in the DAILY-LUMA Cohort. Kidney international reports 3 40303203
2022 Characterization of an induced pluripotent stem cell line (UMi040-A) bearing an auditory neuropathy spectrum disorder-associated variant in TMEM43. Stem cell research 3 35364395
2025 Decreased RYR2 Cluster Size and Abnormal SR Ca2+ Release Contribute to Arrhythmogenesis in TMEM43-Related ARVC. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 2 40948388
2024 Generation of an induced pluripotent stem cell line from a patient with arrhythmogenic right ventricular cardiomyopathy harboring a TMEM43 splice-site variant. Stem cell research 2 38824800
2026 An ARVC-5 Drosophila knock-in model reveals new functions of Tmem43 in lipid homeostasis. Biology open 1 41873591
2026 Newfoundland Mutation TMEM43-p.S358L Causes Impaired Cardiac Energy Metabolism and Mitochondrial Function Through Altered Protein Interaction. Circulation. Genomic and precision medicine 1 41919408
2023 LuMA-Functionalized Thermosensitive Hydrogel: A Versatile and Robust Dopamine-Triggered Platform for Diverse Biomolecules Sensing. ACS applied bio materials 1 37851382
2025 Proteomic screening of TMEM43 binding partners identifies VDAC leading to mitochondrial dysfunction. PloS one 0 41411330

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