Affinage

LEMD2

LEM domain-containing protein 2 · UniProt Q8NC56

Length
503 aa
Mass
57.0 kDa
Annotated
2026-06-10
44 papers in source corpus 20 papers cited in narrative 20 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

LEMD2 (LEM2/NET25) is an inner nuclear membrane protein that anchors chromatin to the nuclear periphery and serves as the site-specific adaptor that recruits the ESCRT-III machinery to seal and repair the nuclear envelope (PMID:28242692, PMID:16339967). Its modular architecture couples distinct activities: an N-terminal LEM motif binds BAF and tethers chromatin, two transmembrane segments and the nucleoplasmic region drive A-type lamin–dependent NE targeting (recruiting emerin, MAN1, and BAF while excluding lamin B), and the C-terminal winged-helix (MSC) domain directly binds and activates CHMP7 to nucleate co-oligomeric ESCRT-III rings (CHMP7, CHMP2A, IST1/CHMP8) at nascent NE holes (PMID:28242692, PMID:16339967). A low-complexity/intrinsically disordered domain confers phase separation and microtubule binding, targeting LEM2 condensation to spindle microtubules so ESCRT recruitment and spindle disassembly are coordinated during NE closure; loss of these activities produces nuclear integrity defects and DNA damage (PMID:32494070). With BAF, LEM2 builds a multivalent protein–DNA surface condensate that mechanically reinforces the envelope and protects DNA under load [PMID:bio_10.1101_2025.05.21.655270]. Beyond sealing, LEM2 organizes peripheral heterochromatin and gene silencing by tethering chromatin and tuning the balance between the SHREC deacetylase complex and the anti-silencing factor Epe1, acting with Nur1 downstream of the H3K9 methyltransferase Clr4 (PMID:26744419, PMID:27451393), and it scaffolds nuclear-periphery RNA surveillance by interacting with the exosome-targeting MTREC/PAXT complex (PMID:36123402). LEM2 also facilitates the replication-stress checkpoint (PMID:26746798) and contributes to nucleotide excision repair at the nuclear periphery (PMID:32085595). Physiologically, LEMD2 is required for development and cardiac genome stability: loss causes nuclear rupture, DNA damage, p53 activation and apoptosis driven by contractile mechanical force, and the LEM-domain p.L13R mutation disrupts BAF binding, impairs NE rupture repair, leaks DNA repair factors, and activates the cGAS/STING/IFN pathway to cause dilated cardiomyopathy (PMID:36377660, PMID:36656972, PMID:37067297).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2005 High

    Established LEMD2's basic architecture and membrane identity — that it is an inner nuclear membrane LEM-domain protein whose envelope targeting depends on A-type lamins and that it organizes other NE proteins.

    Evidence In vitro lamin C binding, subcellular fractionation, and overexpression/domain-truncation immunofluorescence

    PMID:16339967

    Open questions at the time
    • Direct functional consequences of lamin/emerin/MAN1/BAF recruitment not tested
    • No structural detail of the MSC domain
  2. 2009 High

    First functional role: LEMD2 is required for myogenic differentiation and restrains ERK signaling, partly overlapping with emerin but not MAN1.

    Evidence RNAi in C2C12 myoblasts with MEK/ERK pharmacological rescue and silencing-resistant ectopic expression

    PMID:19720741

    Open questions at the time
    • Mechanism linking LEM2 to ERK suppression unresolved
    • Whether the differentiation defect reflects NE integrity or signaling not separated
  3. 2010 Medium

    Defined the chromatin-tethering rule — LEM-2 associates with repeat-dense, H3K27me3-rich chromatin domains based on local chromatin properties rather than chromosomal position.

    Evidence ChIP-seq in C. elegans embryos with a chromosome translocation control

    PMID:21176223

    Open questions at the time
    • Functional consequence of the association not directly tested
    • Reader/recruitment mechanism for the chromatin signature unknown
  4. 2015 High

    Extended LEM2 function to genome maintenance and signaling — it facilitates the Rad3/ATR replication-stress checkpoint and, in mouse, is developmentally essential and modulates MAPK/AKT signaling.

    Evidence S. pombe lem2Δ with checkpoint phosphorylation Western blots and HU sensitivity; Lemd2 knockout mouse (E11.5 lethal) with kinase activation analysis

    PMID:25790465 PMID:26746798

    Open questions at the time
    • How a membrane protein facilitates Rad3 signaling mechanistically unclear
    • Single-lab checkpoint finding
    • Relationship between MAPK regulation and NE roles unresolved
  5. 2016 High

    Resolved domain-specific roles in heterochromatin silencing — the LEM domain tethers chromatin and the MSC domain enforces silencing via the SHREC/Epe1 balance, acting in a Lem2-Nur1 complex downstream of Clr4.

    Evidence Genetic epistasis, ChIP/ChIP-seq, Co-IP, and domain dissection with silencing reporters in S. pombe

    PMID:26744419 PMID:27451393

    Open questions at the time
    • Whether the human ortholog uses the same SHREC/Epe1-equivalent machinery untested
    • Direct MSC-domain partners in silencing not fully defined
  6. 2017 High

    Identified LEM2 as the conserved nuclear ESCRT adaptor — it directly binds CHMP7 through its winged-helix domain and recruits downstream ESCRT-III to seal the nuclear envelope.

    Evidence In vitro direct binding, suppressor/epistasis screen in S. pombe, and RNAi with loss-of-ESCRT-recruitment in human cells

    PMID:28242692

    Open questions at the time
    • Structure of the LEM2-CHMP7 interface not solved
    • Timing/regulation of adaptor engagement during mitotic exit unresolved
  7. 2018 Medium

    Defined how LEM2 is retained at the envelope versus the spindle pole body — Bqt4 competes with the SPB for the N-terminal nucleoplasmic region to keep Lem2 NE-localized.

    Evidence lem2 bqt4 synthetic-lethality genetics, localization microscopy, and domain truncation in S. pombe

    PMID:29292846

    Open questions at the time
    • No metazoan Bqt4 equivalent established
    • Single-lab finding
  8. 2019 Medium

    Showed LEM2 controls nuclear-envelope membrane homeostasis, acting as a barrier to ER membrane flow that sets nuclear size, with Lnp1 as a compensating barrier.

    Evidence Nuclear-size and membrane-flow imaging with lem2 and lem2 lnp1 genetics in S. pombe

    PMID:31015410

    Open questions at the time
    • Molecular basis of the membrane barrier function unknown
    • Conservation in metazoans untested
  9. 2020 High

    Mechanistically unified the sealing pathway and broadened LEM2's roles — phase separation via the LCD targets condensation to spindle microtubules while the winged-helix domain activates CHMP7 ring formation; parallel work tied LEM2 to NER, to ER-membrane restriction during NE closure, and to activity-dependent neuronal nuclear plasticity with SATB2.

    Evidence Phase-separation and microtubule-binding assays, XL-MS and domain mutagenesis (Nature); BioID + UV-C/γH2AX (Cells); C. elegans epistasis with 3D-EM; SATB2 Co-IP with neuronal RNA-seq and nuclear-shape assays

    PMID:32085595 PMID:32271860 PMID:32494070 PMID:33319920

    Open questions at the time
    • How condensation, CHMP7 activation, and chromatin binding are temporally coordinated in vivo not fully integrated
    • NER and SATB2 roles are single-lab, Medium-confidence
  10. 2022 High

    Connected LEMD2 to disease and identified the RNA-surveillance scaffold function — cardiac loss causes DNA-damage-dependent cardiomyopathy via p53, rescuable by gene therapy, and Lem2 recruits exosome substrates to the periphery through MTREC/PAXT.

    Evidence Cardiac cKO and p.L13R knockin mice with AAV rescue and p53/γH2AX readouts; RNA-seq, Co-IP, and substrate localization in S. pombe (MTREC/PAXT)

    PMID:36123402 PMID:36377660

    Open questions at the time
    • Whether RNA surveillance role operates in mammalian cardiomyocytes untested
    • Link between RNA surveillance and genome stability unclear
  11. 2023 High

    Established the mechanism of LEMD2 cardiomyopathy — the p.L13R LEM-domain mutation breaks BAF binding to block NE rupture repair, and contractile mechanical force is the driver of nuclear rupture and cGAS/STING/IFN activation.

    Evidence CRISPR knockin cell/mouse models, LEM2-BAF Co-IP, NE-rupture assays under stiffness/electrical stimulation, myosin/calcium-channel inhibitor rescue, and cGAS/KU80/STING readouts

    PMID:36656972 PMID:37067297

    Open questions at the time
    • Structural basis of the LEM2-BAF interface not solved
    • How impaired repair quantitatively triggers IFN signaling not fully mapped
  12. 2023 Medium

    Identified SUMOylation as a regulatory switch toggling LEM2 between centromere clustering and heterochromatin silencing.

    Evidence Genetic manipulation of SUMO protease Ulp1 localization with lem2 epistasis and clustering/silencing assays in S. pombe

    PMID:37970674

    Open questions at the time
    • SUMO writer/eraser acting on Lem2 not biochemically defined
    • Conservation of the SUMO switch in metazoans untested
  13. 2025 Medium

    Proposed a biophysical reinforcement role — LEM2-BAF form a multivalent protein-DNA surface hydrogel whose IDR-IDR contraction pre-stresses the lamin network and protects DNA under mechanical load.

    Evidence Optical tweezers, AFM, in vitro LEM2-BAF co-condensate reconstitution, IDR mutagenesis, and cellular DNA-damage/micronuclei assays (preprint)

    PMID:bio_10.1101_2025.05.21.655270

    Open questions at the time
    • Preprint, not yet peer-reviewed
    • In vivo demonstration of the surface hydrogel in mammalian nuclei pending

Open questions

Synthesis pass · forward-looking unresolved questions
  • How LEM2's many functions — ESCRT sealing, chromatin silencing, RNA surveillance, checkpoint signaling, and mechanical reinforcement — are integrated and differentially deployed across cell types and conditions remains unresolved.
  • No structural model of the full multifunctional protein in context
  • Mechanism partitioning condensation versus complex assembly in human cells not defined
  • Whether yeast silencing/membrane-flow roles are conserved in mammals largely untested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 3 GO:0003677 DNA binding 2 GO:0042393 histone binding 2 GO:0008092 cytoskeletal protein binding 1
Localization
GO:0000228 nuclear chromosome 3 GO:0005635 nuclear envelope 3 GO:0005783 endoplasmic reticulum 2 GO:0005815 microtubule organizing center 1
Pathway
R-HSA-1852241 Organelle biogenesis and maintenance 4 R-HSA-1643685 Disease 3 R-HSA-4839726 Chromatin organization 3 R-HSA-73894 DNA Repair 1 R-HSA-8953854 Metabolism of RNA 1 R-HSA-8953897 Cellular responses to stimuli 1
Partners
BAFBQT4CHMP7EMERINLAMIN A/CMTREC/PAXTNUR1SATB2
Complex memberships
ESCRT-IIILem2-Nur1 complex

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2017 LEM2 acts as a conserved nuclear site-specific adaptor that directly binds CHMP7 (via its C-terminal winged-helix domain) and recruits downstream ESCRT-III factors (CHMP7, CHMP2A, IST1/CHMP8) to the nuclear envelope during nuclear envelope closure. Genetic epistasis in fission yeast showed lem2 and cmp7 loss-of-function suppresses vps4-deletion nuclear morphology defects, placing them upstream in the same pathway. In vitro direct binding assay (C-terminal domain of LEM2 binds CHMP7), genetic epistasis (suppressor screen in S. pombe), immunofluorescence co-localization in human cells, RNAi knockdown with loss-of-ESCRT-recruitment phenotype Proceedings of the National Academy of Sciences of the United States of America High 28242692
2020 LEM2 undergoes phase separation via its low-complexity domain (LCD), which contains a proline-arginine-rich sequence that binds microtubules and targets LEM2 condensation to spindle microtubules at the nascent nuclear envelope. The LEM motif binds BAF conferring chromatin affinity. The winged-helix domain of LEM2 activates CHMP7 to form co-oligomeric rings. Disruption of phase separation or CHMP7 activation prevented downstream ESCRT recruitment, impaired spindle disassembly, and caused nuclear integrity defects and DNA damage. Phase separation assays, in vitro microtubule binding, domain mutagenesis, cross-linking mass spectrometry (XL-MS), fluorescence microscopy in human cells, loss-of-function phenotypic readouts (DNA damage, spindle disassembly defects) Nature High 32494070
2005 LEM2 is an inner nuclear membrane protein containing an N-terminal LEM motif, two transmembrane domains, and a C-terminal MSC domain. It binds lamin C tail in vitro. Targeting to the nuclear envelope requires A-type lamins and is mediated by the N-terminal and transmembrane domains. Overexpressed LEM2 recruits A-type lamins, emerin, MAN1, and BAF, while excluding lamin B and lamin B receptor. In vitro binding assay (lamin C tail), immunofluorescence of digitonin-treated cells, subcellular fractionation, overexpression/domain truncation analysis Journal of cell science High 16339967
2009 NET25/LEM2 is required for myogenic differentiation of C2C12 myoblasts. RNAi depletion causes hyperactivation of ERK1/2 at the onset of differentiation; pharmacological ERK inhibition rescues myogenesis. Ectopic silencing-resistant NET25 rescues differentiation after emerin depletion, indicating overlapping functions, but does not rescue after MAN1 depletion. RNAi knockdown in C2C12 myoblasts, pharmacological rescue (MEK/ERK inhibitors), ectopic expression of silencing-resistant constructs, differentiation assays Molecular and cellular biology High 19720741
2015 Lemd2 knockout mice die by E11.5. Knockdown of Lem2 in C2C12 myoblasts activates multiple MAP kinases (ERK1/2, JNK, p38) and AKT, indicating Lem2 regulates these signaling pathways. Heterozygous mice show delayed muscle regeneration after cardiotoxin injury. Conditional knockout mouse (homozygous lethal at E11.5), Western blot for activated kinases in knockout embryos and siRNA-treated myoblasts, cardiotoxin muscle regeneration assay PloS one High 25790465
2016 In S. pombe, the LEM domain of Lem2 mediates centromere chromatin binding and perinuclear tethering, while the MSC domain is required for heterochromatin silencing at telomeres and is epistatic with the SHREC (Snf2/HDAC repressor) complex. Loss of Lem2 reduces SHREC association with heterochromatin and increases Epe1 (anti-silencing JmjC protein) binding; these are separable, domain-specific functions. Genetic epistasis (lem2 deletion + SHREC/Epe1 mutant combinations), ChIP, domain deletion/truncation analysis, gene silencing reporter assays in S. pombe Genes & development High 26744419
2016 In S. pombe, Lem2 physically associates with Nur1 (another inner nuclear membrane protein), forming a Lem2-Nur1 complex essential for heterochromatin-mediated gene silencing at centromeres, telomeres, and rDNA. ChIP-seq shows Lem2 binds central core regions of centromeres. Recruitment of Lem2 and Nur1 to silent regions depends on H3K9 methyltransferase Clr4. The complex regulates the balance between SHREC histone deacetylase complex and anti-silencing protein Epe1. Co-immunoprecipitation, ChIP-seq, genetic deletion analysis, silencing reporter assays in S. pombe The Journal of biological chemistry High 27451393
2020 LEM2 has a unique interactome compared to MAN1 and emerin; the LEM2-specific interactome contains nucleotide excision repair (NER) pathway proteins. LEM2-depleted cells (but not MAN1- or emerin-depleted cells) show impaired proliferation after UV-C irradiation and prolonged γH2AX accumulation, indicating a specific role for LEM2 in NER-mediated DNA damage repair at the nuclear periphery. BioID proximity biotinylation interactome, siRNA knockdown, UV-C irradiation assay, γH2AX immunofluorescence Cells Medium 32085595
2020 In C. elegans oocytes, LEM-2 (the LEMD2 ortholog) acts as an NE adaptor for ESCRT-III; loss of NE adaptors (including LEM-2) exacerbates ER membrane invasion into NE holes and nuclear permeability defects caused by loss of the NE phosphatase CNEP-1/CTDNEP1, placing LEM-2/ESCRT-III in a pathway that restricts excess ER membranes during NE closure. Genetic epistasis (double mutant analysis), 3D electron microscopy, nuclear permeability assays in C. elegans embryos The Journal of cell biology Medium 32271860
2022 Cardiac-specific deletion of Lemd2 in mice causes nuclear envelope deformations, extensive DNA damage, apoptosis, and death shortly after birth. Knockin mice carrying the human p.L13R mutation develop dilated cardiomyopathy and cardiac fibrosis. AAV-mediated Lemd2 gene therapy rescued cardiac function in knockin mice, establishing a direct causal link between LEMD2 loss and DNA damage-dependent cardiomyopathy via p53 activation. Conditional cardiac knockout mouse, knockin mouse model (p.L13R), AAV gene therapy rescue, immunostaining for DNA damage markers (γH2AX), apoptosis assays, p53 activation analysis The Journal of clinical investigation High 36377660
2023 The p.L13R mutation in the LEM domain of LEMD2 disrupts the interaction between LEMD2 and BAF (barrier-to-autointegration factor), which is required to initiate the nuclear envelope rupture repair process. Mutant cardiomyocytes show impaired nuclear envelope rupture repair, cytoplasmic leakage of DNA repair factor KU80, increased DNA damage, recruitment of cGAS to nuclear membrane/micronuclei, and activation of the cGAS/STING/IFN pathway promoting premature senescence. CRISPR/Cas9 knockin mouse and cell model, co-immunoprecipitation (LEM2-BAF interaction), nuclear envelope rupture assays under electrical stimulation and substrate stiffness, immunofluorescence for cGAS/KU80/γH2AX, STING pathway activation assays Circulation research High 36656972
2023 In S. pombe, SUMOylation of Lem2 acts as a regulatory switch balancing its roles in centromere clustering versus heterochromatin silencing. Hyper-SUMOylation of Lem2 (caused by delocalizing the SUMO protease Ulp1 from the nuclear envelope) impairs centromeric silencing but enhances centromere clustering; both effects are at least partially dependent on Lem2 SUMOylation. Genetic manipulation of SUMO protease Ulp1 localization, epistasis analysis with lem2 mutants, centromere clustering assays, silencing reporter assays in S. pombe Journal of cell science Medium 37970674
2019 In S. pombe, Lem2 acts as a barrier to membrane flow between the nuclear envelope and the ER; deletion of Lem2 increases membrane flow into and out of the nuclear envelope in response to changes in membrane synthesis and nucleocytoplasmic transport, altering nuclear size. The ER protein Lnp1 acts as a secondary barrier, functionally compensating for loss of Lem2. Fluorescence microscopy of nuclear size in lem2-deletion cells, genetic epistasis (lem2 lnp1 double mutant), membrane flow assays, nuclear size quantification in S. pombe Nature communications Medium 31015410
2018 In S. pombe, Lem2 is retained at the nuclear envelope through its interaction with Bqt4; loss of Bqt4 causes exclusive accumulation of Lem2 at the spindle pole body (SPB). The N-terminal nucleoplasmic region of Lem2 has affinity for both Bqt4 and the SPB in a competitive manner, while the C-terminal region suppresses lem2 bqt4 synthetic lethality. Genetic epistasis (lem2 bqt4 double mutant synthetic lethality), fluorescence microscopy of Lem2 localization in bqt4-deletion cells, domain deletion/truncation analysis in S. pombe Genes to cells : devoted to molecular & cellular mechanisms Medium 29292846
2022 S. pombe Lem2 coordinates nuclear exosome-mediated RNA degradation at the nuclear periphery. Lem2 deletion causes accumulation of RNA precursors and meiotic transcripts. Lem2 does not directly bind RNA but interacts with the exosome-targeting MTREC complex and its human homolog PAXT to promote RNA recruitment to the nuclear periphery. This pathway is regulated by nutrient availability. RNA sequencing (accumulation of RNA precursors in lem2Δ), co-immunoprecipitation (Lem2-MTREC/PAXT interaction), fluorescence microscopy of exosome substrate localization, genetic deletion analysis in S. pombe Nature structural & molecular biology High 36123402
2015 In S. pombe, Lem2 facilitates Rad3 (ATR)-mediated replication checkpoint signaling for Cds1 (CHK2) activation in response to hydroxyurea (nucleotide depletion). In lem2-deletion cells, all Rad3-dependent phosphorylations critical for replication checkpoint signaling are severely compromised, causing aberrant mitosis and drug sensitivity. The DNA damage checkpoint remains largely intact, indicating Lem2 specifically facilitates replication stress checkpoint signaling. Genetic deletion (lem2Δ), Western blotting for checkpoint kinase phosphorylation (Rad3-dependent substrates, Cds1 activation), hydroxyurea sensitivity assay, DNA damage checkpoint analysis in S. pombe Cellular signalling Medium 26746798
2020 SATB2 (a chromosomal scaffolding protein) physically interacts with LEMD2 (inner nuclear membrane protein) in pyramidal neurons, and together they orchestrate activity-dependent nuclear shape changes and gene expression. LEMD2 depletion in cortical neurons affects neuronal activity-dependent regulation of multiple rapid and delayed primary response genes, similar to SATB2 ablation. The activity-driven nuclear envelope plasticity also requires the ESCRT-III/VPS4 complex. Co-immunoprecipitation (SATB2-LEMD2 interaction), siRNA knockdown of LEMD2 in cortical neurons, RNA-seq of activity-regulated genes, in vivo nuclear shape assay (novel environment exposure), immunofluorescence The EMBO journal Medium 33319920
2010 In C. elegans, LEM-2 (LEMD2 ortholog) associates with large chromatin domains on chromosome arms (but not centers) via ChIP, with these domains characterized by high repeat density, low gene density, and H3K27me3 enrichment. A translocated chromosome arm retains LEM-2 association, indicating local chromatin properties (not chromosomal position) primarily determine nuclear membrane interaction. Chromatin immunoprecipitation followed by sequencing (ChIP-seq) in C. elegans embryos, chromosome translocation analysis Genome biology Medium 21176223
2023 Lem2 is essential for cardiac development by protecting cardiomyocyte nuclei from mechanical forces of muscle contraction. Cardiac-specific Lem2 knockout mice show DNA damage, nuclear rupture, and apoptosis driven by muscle contraction (ameliorated by inhibiting myosin contraction and L-type calcium channels). Partial Lem2 depletion (~45%) in adult cardiomyocytes does not cause overt cardiac dysfunction up to 18 months. Conditional cardiac knockout (embryonic and inducible adult), 3D high-resolution episcopic microscopy, RNA-seq, myosin inhibitor/calcium channel blocker rescue, echocardiography, nuclear rupture assays Cardiovascular research High 37067297
2025 LEM2, together with BAF, forms a multivalent protein-DNA co-condensate (surface hydrogel) at the nuclear surface that mechanically reinforces the nuclear envelope and protects DNA under mechanical stress. Under optical tweezer load, the LEM2-BAF assembly induces DNA stiffening beyond its melting point, dependent on LEM2's intrinsically disordered region (IDR). LEM2 IDR-IDR interactions contract the surface hydrogel and introduce pre-stress in the lamin network. Disruption of the surface hydrogel increases DNA damage and micronuclei formation during nuclear deformation. Optical tweezers (single-molecule force spectroscopy), AFM indentation, in vitro reconstitution of LEM2-BAF co-condensates, domain mutagenesis (IDR deletion), live-cell assays for DNA damage and micronuclei bioRxivpreprint Medium bio_10.1101_2025.05.21.655270

Source papers

Stage 0 corpus · 44 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2017 LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission yeast and human cells. Proceedings of the National Academy of Sciences of the United States of America 160 28242692
2010 Caenorhabditis elegans chromosome arms are anchored to the nuclear membrane via discontinuous association with LEM-2. Genome biology 156 21176223
2020 LEM2 phase separation promotes ESCRT-mediated nuclear envelope reformation. Nature 139 32494070
2005 LEM2 is a novel MAN1-related inner nuclear membrane protein associated with A-type lamins. Journal of cell science 126 16339967
2009 Overlapping functions of nuclear envelope proteins NET25 (Lem2) and emerin in regulation of extracellular signal-regulated kinase signaling in myoblast differentiation. Molecular and cellular biology 95 19720741
2016 Control of heterochromatin localization and silencing by the nuclear membrane protein Lem2. Genes & development 94 26744419
2012 Fission yeast Lem2 and Man1 perform fundamental functions of the animal cell nuclear lamina. Nucleus (Austin, Tex.) 87 22540024
2019 Nuclear membrane protein Lem2 regulates nuclear size through membrane flow. Nature communications 64 31015410
2006 The inner nuclear membrane protein Lem2 is critical for normal nuclear envelope morphology. FEBS letters 58 17097643
2020 Regulated lipid synthesis and LEM2/CHMP7 jointly control nuclear envelope closure. The Journal of cell biology 57 32271860
2004 All in the family: evidence for four new LEM-domain proteins Lem2 (NET-25), Lem3, Lem4 and Lem5 in the human genome. Symposia of the Society for Experimental Biology 56 15565891
2019 Characterization of a Unique Form of Arrhythmic Cardiomyopathy Caused by Recessive Mutation in LEMD2. JACC. Basic to translational science 42 31061923
2016 Inner nuclear membrane protein Lem2 augments heterochromatin formation in response to nutritional conditions. Genes to cells : devoted to molecular & cellular mechanisms 42 27334362
2019 The Discovery of a LEMD2-Associated Nuclear Envelopathy with Early Progeroid Appearance Suggests Advanced Applications for AI-Driven Facial Phenotyping. American journal of human genetics 37 30905398
2011 Ce-emerin and LEM-2: essential roles in Caenorhabditis elegans development, muscle function, and mitosis. Molecular biology of the cell 36 22171324
2016 Role of Inner Nuclear Membrane Protein Complex Lem2-Nur1 in Heterochromatic Gene Silencing. The Journal of biological chemistry 34 27451393
2015 Inner nuclear membrane protein LEM-2 is required for correct nuclear separation and morphology in C. elegans. Journal of cell science 33 25653391
2015 Nuclear envelope protein Lem2 is required for mouse development and regulates MAP and AKT kinases. PloS one 31 25790465
2020 Lem2 and Lnp1 maintain the membrane boundary between the nuclear envelope and endoplasmic reticulum. Communications biology 29 32483293
2018 Lem2 is retained at the nuclear envelope through its interaction with Bqt4 in fission yeast. Genes to cells : devoted to molecular & cellular mechanisms 29 29292846
2015 Hutterite-type cataract maps to chromosome 6p21.32-p21.31, cosegregates with a homozygous mutation in LEMD2, and is associated with sudden cardiac death. Molecular genetics & genomic medicine 27 26788539
2017 Nuclear envelope localization of LEMD2 is developmentally dynamic and lamin A/C dependent yet insufficient for heterochromatin tethering. Differentiation; research in biological diversity 23 28056360
2004 A proximal upstream sequence controls tissue-specific expression of Lem2, a salicylate-inducible barley lectin-like gene. Planta 23 15605240
2020 SATB2-LEMD2 interaction links nuclear shape plasticity to regulation of cognition-related genes. The EMBO journal 22 33319920
2022 Loss of function of the nuclear envelope protein LEMD2 causes DNA damage-dependent cardiomyopathy. The Journal of clinical investigation 21 36377660
2020 Comparative Interactome Analysis of Emerin, MAN1 and LEM2 Reveals a Unique Role for LEM2 in Nucleotide Excision Repair. Cells 19 32085595
2023 Mechanistic Insights of the LEMD2 p.L13R Mutation and Its Role in Cardiomyopathy. Circulation research 18 36656972
2023 Lem2 is essential for cardiac development by maintaining nuclear integrity. Cardiovascular research 14 37067297
2016 Beyond Tethering and the LEM domain: MSCellaneous functions of the inner nuclear membrane Lem2. Nucleus (Austin, Tex.) 13 27797637
2022 The inner nuclear membrane protein Lem2 coordinates RNA degradation at the nuclear periphery. Nature structural & molecular biology 12 36123402
2015 Inner nuclear membrane protein Lem2 facilitates Rad3-mediated checkpoint signaling under replication stress induced by nucleotide depletion in fission yeast. Cellular signalling 11 26746798
2023 SUMOylation regulates Lem2 function in centromere clustering and silencing. Journal of cell science 6 37970674
2016 Chromatin binding and silencing: Two roles of the same protein Lem2. Microbial cell (Graz, Austria) 6 28357352
2022 Folic acid-mesoporous silicon nanoparticles enhance the anticancer activity of the p73-activating small molecule LEM2. International journal of pharmaceutics 5 35792422
2019 Identification of the evolutionarily conserved nuclear envelope proteins Lem2 and MicLem2 in Tetrahymena thermophila. Gene: X 5 32550543
2006 The Lem2 gene promoter of barley directs cell- and development-specific expression of gfp in transgenic plants. Plant biotechnology journal 5 17177783
2024 LEMD2-associated progeroid syndrome: Expanding the phenotype of the nuclear envelopathy caused by a defect in LEMD2 gene. Aging cell 3 38757373
2023 The third case of Marbach-Rustad progeroid syndrome caused by a de novo LEMD2 variant. Clinical genetics 3 37867468
2024 Modification of the Trizol Method for the Extraction of RNA from Prorocentrum triestinum ACIZ_LEM2. International journal of molecular sciences 2 39273589
2025 Exploring the roles of Lem2 and Bqt4 in lipid metabolism for nuclear envelope maintenance: a novel perspective. Journal of biochemistry 1 39446564
2024 The expression and role of the Lem-D proteins Ankle2, Emerin, Lemd2, and TMPO in triple-negative breast cancer cell growth. Frontiers in oncology 1 38720803
2026 A muscular dystrophy associated with bi-allelic LEMD2 variants: Expanding the genotype of nuclear envelopathies. Brain pathology (Zurich, Switzerland) 0 41776713
2025 The losses of Lem2 and Bqt4 exhibit similar impacts on intracellular movement dynamics in fission yeast. Biochemical and biophysical research communications 0 39892963
2019 Identification of the evolutionarily conserved nuclear envelope proteins Lem2 and MicLem2 in Tetrahymena thermophila. Gene 0 34530986

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